Halip L.,Timisoara Institute of the Roumanian Academy Chemistry |
Curpn R.,Timisoara Institute of the Roumanian Academy Chemistry |
Borota A.,Timisoara Institute of the Roumanian Academy Chemistry |
Bora A.,Timisoara Institute of the Roumanian Academy Chemistry
Revue Roumaine de Chimie | Year: 2015
Besides the known applications of melatonin which include circadian rhythm's regulation, sleep disorders and depression, recent studies have reported the melatonin implication in cardiovascular regulation, neurodegenerative diseases or cancer treatment. In this light, the melatonin receptors have gained much attention in the last few years, and many drug discovery programs have been focused on the identification of new small molecules which selectively bind to the two melatonin receptor subtypes. In this study, we report the homology modeling of the human melatonin MTR1A based on the crystal structure of the beta1-adrenergic receptor (beta1-AR) receptor, the characterization of the binding site and the most relevant ligand-receptor interactions. Docking simulations revealed an agonist binding mode characterized by interactions with two residues from helix 3, Ser3.35 and Ser 3.39, respectively and a residue from helix 5, His5.46. (Chemical Equation Presented). © 2015, Editions de l'Academie Republique Populaire. All rights reserved.