Muscarinic Receptors: A Comparative Analysis of Structural Features and Binding Modes through Homology Modelling and Molecular Docking Export

@article{citeulike:3795918, abstract = {Three-dimensional models of the five human muscarinic receptors were obtained from their known sequences. Homology modelling based on the crystallographic structure of bovine rhodopsin yielded models compatible with known results from site-directed mutagenesis studies. The only exceptions were the cytoplasmic loop 3 (CL3) in the five receptors, and the large C-terminal domain in M1. Here, homology modelling with other closely related proteins allowed to solve these gaps. A detailed comparative discussion of the five models is given. The second part of the work involved docking experiments with the physiological ligand acetylcholine, again yielding results entirely compatible with results from mutagenesis experiments. The study revealed analogies and differences between the five receptors in the residues, and interactions leading to the recognition and binding of acetylcholine.}, address = {Istituto di Chimica Farmaceutica, Facolt\`{a} di Farmacia, Universit\`{a} di Milano, Viale Abruzzi 42, I-20131 Milano (phone: +39 02 50317545; fax: +39 02 50317565); Department of Pharmacy, University Hospital Centre (CHUV), Rue du Bugnon, CH-1011 Lausanne}, author = {Pedretti, Alessandro and Vistoli, Giulio and Marconi, Cristina and Testa, Bernard}, citeulike-article-id = {3795918}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/cbdv.200690052}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/112635733/ABSTRACT}, doi = {10.1002/cbdv.200690052}, journal = {Chemistry \& Biodiversity}, keywords = {docking, homology\_modeling, muscarinic}, number = {5}, pages = {481--501}, posted-at = {2008-12-16 09:45:15}, priority = {2}, title = {Muscarinic Receptors: A Comparative Analysis of Structural Features and Binding Modes through Homology Modelling and Molecular Docking}, url = {http://dx.doi.org/10.1002/cbdv.200690052}, volume = {3}, year = {2006} }

TY - JOUR ID - citeulike:3795918 L3 - citeulike-article-id:3795918 N2 - Three-dimensional models of the five human muscarinic receptors were obtained from their known sequences. Homology modelling based on the crystallographic structure of bovine rhodopsin yielded models compatible with known results from site-directed mutagenesis studies. The only exceptions were the cytoplasmic loop 3 (CL3) in the five receptors, and the large C-terminal domain in M1. Here, homology modelling with other closely related proteins allowed to solve these gaps. A detailed comparative discussion of the five models is given. The second part of the work involved docking experiments with the physiological ligand acetylcholine, again yielding results entirely compatible with results from mutagenesis experiments. The study revealed analogies and differences between the five receptors in the residues, and interactions leading to the recognition and binding of acetylcholine. IS - 5 JF - Chemistry & Biodiversity AD - Istituto di Chimica Farmaceutica, Facoltà di Farmacia, Università di Milano, Viale Abruzzi 42, I-20131 Milano (phone: +39 02 50317545; fax: +39 02 50317565); Department of Pharmacy, University Hospital Centre (CHUV), Rue du Bugnon, CH-1011 Lausanne EP - 501 TI - Muscarinic Receptors: A Comparative Analysis of Structural Features and Binding Modes through Homology Modelling and Molecular Docking VL - 3 SP - 481 KW - docking KW - homology_modeling KW - muscarinic AU - Pedretti, Alessandro AU - Vistoli, Giulio AU - Marconi, Cristina AU - Testa, Bernard PY - 2006/// UR - http://dx.doi.org/10.1002/cbdv.200690052 ER -