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Structural Biology

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The structural biology & molecular modeling techniques market is expected to reach USD 13.1 billion by 2025. An unprecedented rise in the adoption of unhealthy lifestyles has led to an upsurge in the prevalence of chronic diseases, such as diabetes and cancer, which is presumed to propel the structural biology & molecular modeling techniques market during the forecast period. Moreover, increasing drug resistance coupled with the high drug attrition rate is engendering the requirement for extensive R&D activities, which is presumed to boost the adoption of structural biology & molecular modeling techniques in the drug discovery and development process. This is expected to serve as an efficient approach in fast tracking the development of drugs with high potency. The heightening demand for molecular modeling techniques is predominantly attributable to the significant cost reduction enabled. This is due to the fact that prediction software identifies possible adverse reactions and determines drug efficacy and toxicity in the pre-clinical stages, thereby reducing the probability of drug failure at the later stages. Consequentially, the aforementioned factors serve as prominent reasons responsible for the widened market demand. Further key findings from the study suggest: Key Topics Covered: 1 Research Methodology & Scope 2 Executive Summary 3 Structural Biology & Molecular Modeling Techniques Market Variables, Trends & Scope 3.1 Market Segmentation & Scope 3.2 Market Driver Analysis 3.3 Market Restraint Analysis 3.4 Penetration & Growth Prospect Mapping 3.5 Structural Biology And Molecular Modeling Techniques - SWOT Analysis, By Factor (political & legal, economic and technological) 3.6 Industry Analysis - Porter's 4 Structural Biology & Molecular Modeling Techniques Market: Tools Estimates & Trend Analysis 4.1 Structural biology & molecular modeling techniques market: Tools movement analysis 4.2 SaaS & Stand-Alone Modeling Software 4.2.2 Homology Modeling 4.2.3 Threading 4.2.4 Molecular Dynamics 4.2.5 Ab Initio 4.2.6 Hybrid 4.2.7 Others 4.3 Visualization & Analysis Software 4.4 Databases 4.5 Others 5 Structural Biology & Molecular Modeling Techniques Market: Application Estimates & Trend Analysis 5.1 Structural Biology & Molecular Modeling Techniques Market: Application Movement Analysis 5.2 Drug Development 5.3 Drug Discovery 5.4 Others 6 Structural Biology & Molecular Modeling Techniques: Regional Estimates & Trend Analysis, by Tools, Application 7 Competitive Landscape For more information about this report visit http://www.researchandmarkets.com/research/3wjzxc/structural Research and Markets Laura Wood, Senior Manager press@researchandmarkets.com For E.S.T Office Hours Call +1-917-300-0470 For U.S./CAN Toll Free Call +1-800-526-8630 For GMT Office Hours Call +353-1-416-8900 U.S. Fax: 646-607-1907 Fax (outside U.S.): +353-1-481-1716 To view the original version on PR Newswire, visit:http://www.prnewswire.com/news-releases/global-structural-biology--molecular-modeling-techniques-market-analysis-2014-2017--2025---research-and-markets-300444153.html


DUBLIN, Apr. 25, 2017 /PRNewswire/ -- Research and Markets has announced the addition of the "Structural Biology & Molecular Modeling Techniques Market Analysis By Tools, By Application And Segment Forecasts 2014 - 2025" report to their offering. The structural biology &...


AIIMS and CSIR IGIB Ink Deal for Partnership in Clinical and Translational Genomics, Expanding on Reach of the GUaRDIAN Programme The All India Institute of Medical Sciences (AIIMS) Delhi and CSIR Institute of Genomics and Integrative Biology (CSIR-IGIB) inked a deal for collaborative research in the area of Rare Diseases and application of genomics to aid clinical decisions, expanding on the reach of the GUaRDIAN programme. New Delhi, India, May 28, 2017 --( AIIMS Delhi is a premier Institute for medical education and research in India, having extraordinary infrastructure, specialized medical/paramedical staff, management and state of the art facilities for patient care, training programmes and research activities. CSIR-IGIB is one of the premier Institutes in India pioneering cutting edge advancements in Genomic Science and a constituent laboratory of the Council for Scientific and Industrial Research (CSIR). Research at CSIR-IGIB spans a variety of areas including Genomics & Molecular Medicine, Chemical & Systems Biology, Genome Informatics & Structural Biology, Respiratory Disease Biology and Energy & Environmental Biotechnology. As part of the agreement, AIIMS Delhi and CSIR IGIB would collaborate in the area of genetic diseases as well as application of genomics in clinical settings. This would include formulation and participation in joint collaborative programs spanning genomics for aiding the diagnosis, understanding the prognosis and aiding precise therapy of genetic diseases. The deal would also enable faculty members of both institutes to actively participate in formulating and implementing collaborative programs aimed at accelerating the application of genomics to aid clinical decisions. The deal would also allow AIIMS Delhi to access the state of the art genomics and bioinformatics infrastructure as well as the clinical genomics analytical resources at CSIR IGIB to enable fast, accurate and cost effective diagnosis of genetic diseases for patients coming to AIIMS Delhi. CSIR IGIB has been a pioneer in translational genomics in India. The Genomics for Understanding Rare Diseases India Alliance Network (GUaRDIAN) is a focussed translational research programme in the area of Rare Diseases initiated in the year 2015. The programme has evolved to become one of the largest of its kind in the area of Rare genetic diseases with a clinical collaborative network of over 100 clinicians from over 35 clinical centres across India working on Rare Diseases. A complementary programme entitled Genomics and other Omics tools for Enabling Medical Decisions (GOMED) initiated last year at CSIR IGIB enables affordable and equitable access to genetic diagnosis. The programme covers genetic tests for over 80 genes and has already catered to over 2000 patients in from over 25 Centres from across India. Skilled manpower is undoubtedly essential to advance and accelerate clinical adoption of genomics. This deal also envisages imparting genomics knowledge for practicing clinicians through training and education as well as faculty exchange. This would surely provide impetus to national initiatives like the Skill India programme. The deal also envisages setting up collaborative research programmes aimed at accelerating research in the area of clinical genomics in India. New Delhi, India, May 28, 2017 --( PR.com )-- The All India Institute of Medical Sciences (AIIMS) Delhi and CSIR Institute of Genomics and Integrative Biology (CSIR-IGIB) inked a deal for collaborative research in the area of Rare Diseases and application of genomics to aid clinical decisions.AIIMS Delhi is a premier Institute for medical education and research in India, having extraordinary infrastructure, specialized medical/paramedical staff, management and state of the art facilities for patient care, training programmes and research activities. CSIR-IGIB is one of the premier Institutes in India pioneering cutting edge advancements in Genomic Science and a constituent laboratory of the Council for Scientific and Industrial Research (CSIR). Research at CSIR-IGIB spans a variety of areas including Genomics & Molecular Medicine, Chemical & Systems Biology, Genome Informatics & Structural Biology, Respiratory Disease Biology and Energy & Environmental Biotechnology.As part of the agreement, AIIMS Delhi and CSIR IGIB would collaborate in the area of genetic diseases as well as application of genomics in clinical settings. This would include formulation and participation in joint collaborative programs spanning genomics for aiding the diagnosis, understanding the prognosis and aiding precise therapy of genetic diseases. The deal would also enable faculty members of both institutes to actively participate in formulating and implementing collaborative programs aimed at accelerating the application of genomics to aid clinical decisions.The deal would also allow AIIMS Delhi to access the state of the art genomics and bioinformatics infrastructure as well as the clinical genomics analytical resources at CSIR IGIB to enable fast, accurate and cost effective diagnosis of genetic diseases for patients coming to AIIMS Delhi.CSIR IGIB has been a pioneer in translational genomics in India. The Genomics for Understanding Rare Diseases India Alliance Network (GUaRDIAN) is a focussed translational research programme in the area of Rare Diseases initiated in the year 2015. The programme has evolved to become one of the largest of its kind in the area of Rare genetic diseases with a clinical collaborative network of over 100 clinicians from over 35 clinical centres across India working on Rare Diseases.A complementary programme entitled Genomics and other Omics tools for Enabling Medical Decisions (GOMED) initiated last year at CSIR IGIB enables affordable and equitable access to genetic diagnosis. The programme covers genetic tests for over 80 genes and has already catered to over 2000 patients in from over 25 Centres from across India.Skilled manpower is undoubtedly essential to advance and accelerate clinical adoption of genomics. This deal also envisages imparting genomics knowledge for practicing clinicians through training and education as well as faculty exchange. This would surely provide impetus to national initiatives like the Skill India programme. The deal also envisages setting up collaborative research programmes aimed at accelerating research in the area of clinical genomics in India.


DUBLIN--(BUSINESS WIRE)--Research and Markets has announced the addition of the "Structural Biology & Molecular Modeling Techniques Market Analysis By Tools, By Application And Segment Forecasts 2014 - 2025" report to their offering. The structural biology & molecular modeling techniques market is expected to reach USD 13.1 billion by 2025 An unprecedented rise in the adoption of unhealthy lifestyles has led to an upsurge in the prevalence of chronic diseases, such as diabetes and cancer, which is presumed to propel the structural biology & molecular modeling techniques market during the forecast period. Moreover, increasing drug resistance coupled with the high drug attrition rate is engendering the requirement for extensive R&D activities, which is presumed to boost the adoption of structural biology & molecular modeling techniques in the drug discovery and development process. This is expected to serve as an efficient approach in fast tracking the development of drugs with high potency. The heightening demand for molecular modeling techniques is predominantly attributable to the significant cost reduction enabled. This is due to the fact that prediction software identifies possible adverse reactions and determines drug efficacy and toxicity in the pre-clinical stages, thereby reducing the probability of drug failure at the later stages. Consequentially, the aforementioned factors serve as prominent reasons responsible for the widened market demand. For more information about this report visit http://www.researchandmarkets.com/research/fxhk2b/structural


News Article | February 22, 2017
Site: www.eurekalert.org

A Phase 1 clinical trial to test the safety and tolerability of an investigational vaccine against respiratory syncytial virus (RSV) has begun at the National Institutes of Health Clinical Center in Bethesda, Maryland. The trial also will assess the vaccine's ability to prompt an immune response in healthy adult participants. The investigational vaccine was developed by scientists at the National Institute of Allergy and Infectious Diseases (NIAID), part of NIH. Most people are infected with RSV by age 2 and undergo repeated infections throughout life. Infected adults and children generally experience mild, cold-like symptoms that resolve within a week or two. However, infection can cause severe lower respiratory tract disease, including pneumonia and bronchiolitis, among premature infants, children younger than age 2 with heart or lung problems, children and adults with weakened immune systems and the elderly. About 2 percent of RSV-infected infants under 1 year of age require hospitalization. Children between ages 1 and 5 years and adults older than 65 years are also at higher risk of hospitalization. Each year on average in the United States, RSV leads to 57,527 hospitalizations and 2.1 million outpatient visits among children younger than 5 years; and 177,000 hospitalizations and 14,000 deaths among adults older than 65 years, according to the Centers for Disease Control and Prevention. Globally, RSV infections are estimated to cause more than 250,000 deaths each year. Currently no vaccine to prevent RSV infection or drug to treat it is available. The monoclonal antibody palivizumab is licensed in the U.S. for preventing serious lower respiratory tract disease caused by RSV in high-risk children, but it is not licensed for use in the general population. "RSV is underappreciated as a major cause of illness and death, not only in infants and children but also in people with weakened immune systems and the elderly," said NIAID Director Anthony S. Fauci, M.D. "A vaccine to reduce the burden of this important disease is badly needed." The study, called VRC 317, will enroll healthy adults ages 18-50 years. Participants will be randomly assigned to receive two injections in the arm at 12 weeks apart with either the investigational vaccine or the investigational vaccine adjuvanted with alum. Alum is a chemical compound commonly added to vaccines to enhance the body's immune response. Participants will also be randomly assigned to receive one of three vaccine doses (50 micrograms, 150 micrograms or 500 micrograms) at both vaccination time points. Initially, five people will be vaccinated with the 50 microgram dose. If the initial group of participants experience no serious adverse reactions attributable to the vaccine, the study team will then begin to vaccinate participants at the next dosage level. They will repeat this stepwise process until they administer the 500 microgram dose. Participants will return for 12 clinic visits over 44 weeks after the first injection. At these visits, study clinicians will conduct physical exams and collect blood samples. They will also test mucous samples from volunteers' mouths and noses to measure the immune responses generated. The study is being led by principal investigator Michelle C. Crank, M.D., head of the Translational Sciences Core in the Viral Pathogenesis Laboratory part of NIAID's Vaccine Research Center (VRC). Study clinicians will conduct a daily safety review of any new clinical information, and a Protocol Safety Review Team will examine trial safety data weekly to ensure the vaccine meets safety standards. The investigational vaccine, called DS-Cav1, results from years of research led by Barney S. Graham, M.D., Ph.D., deputy VRC director, and Peter D. Kwong, Ph.D., chief of the Structural Biology Section and the Structural Bioinformatics Core at the VRC. The vaccine candidate is a single, structurally-engineered protein from the surface of RSV rather than a more traditional approach based on a weakened or inactivated whole virus. In 2013, VRC scientists tested several versions of the protein as a vaccine in mice and nonhuman primates. The protein variants elicited high levels of neutralizing antibodies and protected the animals against RSV infection. Drs. Graham and Kwong selected the most promising candidate, DS-Cav1, for clinical evaluation. "This work represents an example of how new biological insights from basic research can lead to candidate vaccines for diseases of public health importance, and the value of multidisciplinary research teams like the ones assembled at the VRC," said Dr. Graham. The trial is expected to take one year to complete. For more information about the trial, visit clinicaltrials.gov and search identifier NCT03049488. For more information, visit about NIAID's Respiratory Syncytial Virus (RSV) web page. NIAID conducts and supports research--at NIH, throughout the United States, and worldwide--to study the causes of infectious and immune-mediated diseases, and to develop better means of preventing, diagnosing and treating these illnesses. News releases, fact sheets and other NIAID-related materials are available on the NIAID website. About the National Institutes of Health (NIH): NIH, the nation's medical research agency, includes 27 Institutes and Centers and is a component of the U.S. Department of Health and Human Services. NIH is the primary federal agency conducting and supporting basic, clinical, and translational medical research, and is investigating the causes, treatments, and cures for both common and rare diseases. For more information about NIH and its programs, visit http://www. .


SAN DIEGO--(BUSINESS WIRE)--Ligand Pharmaceuticals Incorporated (NASDAQ: LGND) announces the appointment of Christel Iffland, Ph.D. as a Vice President of Antibody Technologies. Dr. Iffland joins Ligand from Merck KGaA/EMD Serono where she served as Group Leader of Antibody Display Technologies, a Senior Scientist of Phage Technologies and Structural Biology and Associate Director of Antibody Technologies. At Ligand, Dr. Iffland will support current and new partnerships and collaborations for the OmniAb franchise, providing scientific guidance and input. Additionally, she will contribute to the continued growth and next-generation innovation of OmniAb and to the technical assessment of new opportunities. “Christel has been a longtime user of the OmniAb technology and we are delighted to welcome her to Ligand as we further expand our scientific team focused on antibodies and antibody technologies,” said John Higgins, Ligand’s Chief Executive Officer. “Our acquisition of the OmniAb technology last year transformed and expanded Ligand’s business model. Antibody treatments are the fastest-growing segment of the pharmaceutical industry and will continue to be an important area of focus for Ligand as we expand our portfolio of more than 150 fully-funded shots-on-goal.” Dr. Iffland received her Ph.D. in Molecular and Cell Biology from the Université de Nice Sophia-Antipolis in Nice, France and completed post-doctoral research training at both the Dana-Farber Cancer Institute at Harvard Medical School and the Albert Einstein College of Medicine. Dr. Iffland is an author of numerous scientific publications and patents and is a prior recipient of the Merck Award for Patent and Inventorship. OmniAb includes three transgenic animal platforms for producing mono- and bispecific human therapeutic antibodies. OmniRat® is the industry’s first human monoclonal antibody technology based on rats. It has a complete immune system with a diverse antibody repertoire and generates antibodies with human idiotypes as effectively as wild-type animals make rat antibodies. OmniMouse® is a transgenic mouse that complements OmniRat and expands epitope coverage. OmniFlic® is an engineered rat with a fixed light chain for development of bispecific, fully human antibodies. The three platforms use patented technology, have broad freedom to operate and deliver fully human antibodies with high affinity, specificity, expression, solubility and stability. Ligand is a biopharmaceutical company focused on developing or acquiring technologies that help pharmaceutical companies discover and develop medicines. Our business model creates value for stockholders by providing a diversified portfolio of biotech and pharmaceutical product revenue streams that are supported by an efficient and low corporate cost structure. Our goal is to offer investors an opportunity to participate in the promise of the biotech industry in a profitable, diversified and lower-risk business than a typical biotech company. Our business model is based on doing what we do best: drug discovery, early-stage drug development, product reformulation and partnering. We partner with other pharmaceutical companies to leverage what they do best (late-stage development, regulatory management and commercialization) to ultimately generate our revenue. Ligand’s Captisol® platform technology is a patent-protected, chemically modified cyclodextrin with a structure designed to optimize the solubility and stability of drugs. OmniAb® is a patent-protected transgenic animal platform used in the discovery of fully human mono-and bispecific therapeutic antibodies. Ligand has established multiple alliances, licenses and other business relationships with the world's leading pharmaceutical companies including Novartis, Amgen, Merck, Pfizer, Celgene, Gilead, Janssen, Baxter International and Eli Lilly. This news release contains forward-looking statements by Ligand that involve risks and uncertainties and reflect Ligand's judgment as of the date of this release. Actual events or results may differ from our expectations. For example, there can be no assurances that Ligand will be able to develop a next-generation OmniAb technology or that the antibody treatments will continue to be the fastest-growing segment of the pharmaceutical industry. The failure to meet expectations with respect to any of the foregoing matters may reduce Ligand's stock price. Additional information concerning these and other important risk factors affecting Ligand can be found in Ligand's prior press releases available at www.ligand.com as well as in Ligand's public periodic filings with the Securities and Exchange Commission, available at www.sec.gov. Ligand disclaims any intent or obligation to update these forward-looking statements beyond the date of this press release, except as required by law. This caution is made under the safe harbor provisions of the Private Securities Litigation Reform Act of 1995.


News Article | February 15, 2017
Site: phys.org

Multi-drug resistance in bacteria has been identified as a major worldwide public health concern by the World Health Organization.  Multi-drug resistant bacteria are responsible for approximately 700,000 deaths per year, a figure which the WHO says could reach 10 million by the year 2050. EptA causes multi-drug resistance by masking bacteria against both the human immune system and important classes of antibiotics. A very similar variant of EptA called MCR-1 was discovered in 2015 causing resistance to colistin, a last resort antibiotic for bacteria untreatable by other means. Alarmingly, MCR-1 is not limited to a single type of bacteria, but is able to spread between different species of bacteria increasing its harmfullness significantly. Lead scientist in the study, Professor of Structural Biology Alice Vrielink from UWA's School of Molecular Sciences, said the researchers used a technique called X-ray crystallography to map three-dimensional shape of EptA. "The function of a protein molecule is directly related to it's three-dimensional shape," Professor Vrielink said. "This new knowledge of the shape and unique structure of EptA (and MCR-1) will help scientists develop an effective treatment to prevent antibiotic resistance of these super bugs, a huge step forward for global health." Work towards identifying potential new therapuetic molecules targeting EptA and MCR-1 is already underway through joint efforts by researchers at the UWA School of Molecular Sciences, the Marshall Center for Infectious Disease and the Monash Institute of Pharmaceutical Sciences. The research is funded by National Health and Medical Research Council of Australia and included collaborations from several universities and organisations around the globe. The research has been published in the journal Proceedings of the National Academy of Sciences (PNAS). Explore further: Antibiotics can still kill drug-resistant bacteria if they 'push' hard enough into bacterial cells More information: Anandhi Anandan et al. Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding, Proceedings of the National Academy of Sciences (2017). DOI: 10.1073/pnas.1612927114


News Article | November 29, 2016
Site: www.eurekalert.org

The Fas protein can either inhibit or promote the controlled cell death (apoptosis), depending on the isoform in which it occurs. Together with international colleagues, researchers from the Helmholtz Zentrum München and the Technical University of Munich have elucidated how this decision is guided. These results provide new insights into the molecular mechanisms of tumor diseases and have now been published in eLife. Please find a video of the PI explaining the story here: https:/ We know the problem: When assembling the parts and pieces of furniture purchased at a store, everyone uses the same blueprint. Nevertheless, the end product can differ greatly in the course of assembling the whole product over several intermediate steps. Something quite similar can happen during the production of proteins from genes. The genome (the blueprint) is first transcribed into a messenger molecule, the mRNA, and then translated into proteins (furniture). However, the mRNA can be altered and trimmed during intermediate steps in a process called alternative splicing, so that ultimately different proteins are produced from the same blueprint. An interesting example of alternative splicing is the mRNA of the Fas gene*. Depending on which intermediate steps take place, the finished protein can either prevent or promote controlled cell death (apoptosis). "The right balance between these opposing results is dependent on the cell type and can also lead to uncontrolled cell growth and cancer when alternative splicing is dysregulated," explains Professor Michael Sattler, Director of the Institute of Structural Biology (STB) at Helmholtz Zentrum München. In collaboration with Professor Juan Valcárcel Juárez of the Centre de Regulació Genòmica (CRG) in Barcelona, he and his team have now gained insight into which intermediate steps are taken and how these lead to different isoforms of the Fas protein. "The focus of our interest was the protein RBM5, which often exhibits mutations in lung tumors," says Dr. André Mourão of the STB. "RBM5 helps to bring the spliceosome to the mRNA by binding to a spliceosomal protein", explains coauthor Dr. Sophie Bonnal of the CRG Barcelona. In this central position, RBM5 decides which isoform of Fas is expressed and thus controls the balance between the two different isoforms.** "By employing nuclear magnetic resonance (NMR) spectroscopy at the Bavarian NMR Center in Garching, we were able to elucidate the spatial structure of RBM5-OCRE in complex with SmN (a protein present in the spliceosome) and to understand exactly how these interaction occurs," states Sattler, who directed the study.*** To confirm their findings, the scientists mutated the corresponding interaction residues of the proteins and observed that the interactions no longer took place in the test tube and that the splicing activities of RBM5 in cell culture was impaired. "The process of alternative splicing affects numerous essential functions and processes in an organism, and dysregulation can trigger cancer. That is why it is very important to precisely understand the mechanisms that regulate these processes," explains Sattler, summarizing the results. According to the authors, only a few protein interactions that influence alternative splicing by binding to spliceosomal proteins have been analyzed in such structural depth. In the future, the researchers want to determine exactly how RBM5 binds to the mRNA and whether there are additional interactions with the spliceosome, which consists of numerous other components. * Fas is also known as CD95 or APO-1. Depending on whether a specific region (exon 6) is contained in the mRNA or not, a membrane-bound pro-apoptotic protein or a soluble isoform arises in the cell interior, which counteracts apoptosis. As a pro-apoptotic protein, Fas prevents errant cells from multiplying uncontrolled, whereas the anti-apoptotic isoform leads to the proliferation of such cells. ** The name is an acronym for RNA Binding Motif 5. RBM5 is a protein, which is demonstrably dysregulated in different cancers (especially in the lungs). *** A so-called OCRE (octamer repeat of aromatic residues) domain of the protein RBM5 binds to the C-terminus of the spliceosomal protein SmN and is thus important for the regulation of the alternative splicing. Background: In addition to his work at Helmholtz Zentrum München, Prof. Dr. Sattler holds the chair of Biomolecular NMR Spectroscopy at Technische Universität München. He heads the Bavarian NMR Center, which is jointly operated by TUM and HMGU (http://www. ). The Institució Catalana de Recerca i Estudis Avançats (ICREA) in Barcelona in Spain (http://www. ) and the Institut de Génétique Moléculaire de Montpellier in France also participated in the study. Publication: Mourão, A. & Bonnal, S. & Soni, K. & Warner, L. et al. (2016): Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation. eLife, doi: 10.7554/eLife.14707 https:/ The Helmholtz Zentrum München, the German Research Center for Environmental Health, pursues the goal of developing personalized medical approaches for the prevention and therapy of major common diseases such as diabetes and lung diseases. To achieve this, it investigates the interaction of genetics, environmental factors and lifestyle. The Helmholtz Zentrum München is headquartered in Neuherberg in the north of Munich and has about 2,300 staff members. It is a member of the Helmholtz Association, a community of 18 scientific-technical and medical-biological research centers with a total of about 37,000 staff members. http://www. The Institute for Structural Biology (STB) investigates the spatial structures of biological macromolecules, their molecular interactions and dynamics using integrated structural biology by combining X-ray crystallography, NMR-spectroscopy and other methods. Researchers at STB also develop NMR spectroscopy methods for these studies. The goal is to unravel the structural and molecular mechanisms underlying biological function and their impairment in disease. The structural information is used for the rational design and development of small molecular inhibitors in combination with chemical biology approaches. http://www. Technical University of Munich (TUM) is one of Europe's leading research universities, with more than 500 professors, around 10,000 academic and non-academic staff, and 40,000 students. Its focus areas are the engineering sciences, natural sciences, life sciences and medicine, combined with economic and social sciences. TUM acts as an entrepreneurial university that promotes talents and creates value for society. In that it profits from having strong partners in science and industry. It is represented worldwide with a campus in Singapore as well as offices in Beijing, Brussels, Cairo, Mumbai, San Francisco, and São Paulo. Nobel Prize winners and inventors such as Rudolf Diesel, Carl von Linde, and Rudolf Mößbauer have done research at TUM. In 2006 and 2012 it won recognition as a German "Excellence University." In international rankings, TUM regularly places among the best universities in Germany. http://www. Contact for the media: Department of Communication, Helmholtz Zentrum München - German Research Center for Environmental Health, Ingolstädter Landstr. 1, 85764 Neuherberg - Tel. +49 89 3187 2238 - Fax: +49 89 3187 3324 - E-mail: presse@helmholtz-muenchen.de Scientific Contact at Helmholtz Zentrum München: Prof. Dr. Michael Sattler, Helmholtz Zentrum München - German Research Center for Environmental Health, Institute for Structural Biology, Ingolstädter Landstraße 1, 85764 Neuherberg, Tel. +49 89 3187 3800, E-mail: sattler@helmholtz-muenchen.de


Spurlino J.C.,Structural Biology
Methods in Enzymology | Year: 2011

Abstract We screen for fragments using X-ray crystallography as the primary screen. There are several unique features in our screening methodology. As a result of using X-ray diffraction as our primary screen, we do not use affinity data to bias our data collection or design in progressing hits toward a lead. Another difference in our methodology is that we choose to group our compounds as shape-similar groups. We also screen in a first pass mode without recollecting failed diffraction experiments. This method of screening results in an average loss of 510% of the data sets for the primary screen. The remaining data sets offer enough information to successfully advance three to five scaffolds into the secondary library design. We do not deconvolute the wells which show evidence of fragment binding by repeating the soaks with single compounds. Instead, evaluation of the possible fragments is done by refinement and examination of the resulting electron density difference maps. These methods allow us to complete the initial screen of a primary library of fragments in less than 3 months. A secondary library of fragments is designed using the base structures with electron density envelopes from the successful fragment hits of the primary library. Chemistry is chosen to probe interactions with the target and push the observed binding pocket limits in order to more clearly define the plasticity and range of possible extensions to the scaffolds chosen. The secondary library compounds are also screened in shape-similar groupings of five that are chosen without the knowledge of binding affinity. Our approach is a completely orthogonal one from traditional high-throughput screening in finding novel compounds. © 2011 Elsevier Inc.


News Article | November 11, 2016
Site: phys.org

New work by a team of researchers based at The Rockefeller University has determined the structure of one important component of the restrictive gate through which cargo, including genetic information in the form of RNA transcribed from DNA, must pass. The results were published November 10 in Cell. After cells make an RNA version of DNA, they must package it, and ship it through a portal known as the nuclear pore. Once on the other side, some of that packaging has to come off. "We already understood bits and pieces of this aspect of flux into and out of the nucleus, but not the complete picture," says co-corresponding author Brian T. Chait's Laboratory of Mass Spectrometry and Gaseous Ion Chemistry. "To better understand the end of RNA's journey through the pore, we examined the protein complex responsible for receiving RNA and helping to unwrap it," says co-corresponding author Michael P. Rout, head of the Laboratory of Cellular and Structural Biology. "Next, we determined how this structure attached to the rest of the nuclear pore." Scientists typically crystallize proteins in order to determine their structure. But that approach didn't work well for this component because it is relatively large and has flexible parts. So the team pieced a variety of data together as if assembling a jigsaw puzzle. They found that the core of the complex takes a triangular shape, shown in solid red in the image above. This triangle sits atop a Y-shaped piece, shown in lighter red, creating an arm that extends, cranelike, over the pore. This configuration came as a surprise; previously these proteins were thought to stick out further from the pore, like antennae. Although the team performed their research on yeast, their work likely has relevance for humans, who possess a similar protein complex. In humans, mutations that affect the complex, as well as other parts of the RNA-catching arm, have been linked to cancer and other diseases. This new blueprint may help to explain why these mutations are harmful, the researchers say. Explore further: Parasites reveal how evolution has molded an ancient nuclear structure More information: Javier Fernandez-Martinez et al. Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform, Cell (2016). DOI: 10.1016/j.cell.2016.10.028

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