Entity

Time filter

Source Type


De Gieter S.,Vrije Universiteit Brussel | De Gieter S.,Molecular Recognition Unit MoRe | Konijnenberg A.,University of Antwerp | Talavera A.,Vrije Universiteit Brussel | And 11 more authors.
Journal of Biological Chemistry | Year: 2014

The toxin Doc from the phd/doc toxin-antitoxin module targets the cellular translation machinery and is inhibited by its antitoxin partner Phd. Here we show that Phd also functions as a chaperone, keeping Doc in an active, correctly folded conformation. In the absence of Phd, Doc exists in a relatively expanded state that is prone to dimerization through domain swapping with its active site loop acting as hinge region. The domain-swapped dimer is not capable of arresting protein synthesis in vitro, whereas the Doc monomer is. Upon binding to Phd, Doc becomes more compact and is secured in its monomeric state with a neutralized active site. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Source


Vuchelen A.,Vrije Universiteit Brussel | Vuchelen A.,Molecular Recognition Unit MoRe | Pardon E.,Vrije Universiteit Brussel | Pardon E.,Molecular Recognition Unit MoRe | And 13 more authors.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications | Year: 2013

The VAR2CSA protein has been closely associated with pregnancy-associated malaria and is recognized as the main adhesin exposed on the surface of Plasmodium falciparum-infected erythrocytes. Chondroitin sulfate A was identified as the main host receptor in the placenta. Single-domain heavy-chain camelid antibodies, more commonly called nanobodies, were selected and produced against the DBL6-FCR3 domain of VAR2CSA. Crystals of two specific nanobodies, Nb2907 and Nb2919, identified as strong binders to DBL6-FCR3 and the full-length VAR2CSA exposed on the surface of FCR3 P. falciparum-infected erythrocytes, were obtained. Crystals of Nb2907 diffract to 2.45Å resolution and belong to space group C2 with unit-cell parameters a = 136.1, b = 78.5, c = 103.4Å, β = 118.8°, whereas Nb2919 crystals diffract to 2.15Å resolution and belong to space group P43212 with unit-cell parameters a = b = 62.7, c = 167.2Å. © 2013 International Union of Crystallography All rights reserved. Source

Discover hidden collaborations