Authors

Mayako Michino, Scripps Research Institute
Enrique Abola, Scripps Research Institute
Charles L. Brooks, University of Michigan, Ann Arbor
J. Scott Dixon, Daylight Chemical Information Systems, Inc.
John Moult, University System of Maryland
Raymond C. Stevens, Scripps Research Institute
Arthur Olson, Scripps Research Institute
Wiktor Jurkowski, Stockholms universitet
Arne Elofsson, Stockholms universitet
Slawomir Filipek, International Institute of Molecular and Cell Biology
Irina Pogozheva, University of Michigan, Ann Arbor
Andrei Lomize, University of Michigan, Ann Arbor
Bernard Maigret, LORIA Laboratoire Lorrain de Recherche en Informatique et ses Applications
Jeremy Horst, University of Washington, Seattle
Ambrish Roy, University of Kansas
Brady Bernard, University of Washington, Seattle
Shyamala Iyer, University of Washington, Seattle
Yang Zhang, University of Kansas
Ram Samudrala, University of Washington, Seattle
Osman Ugur Sezerman, Sabancı Üniversitesi
Gregory V. Nikiforovich, University of Washington, Seattle
Christina M. Taylor, University of Washington, Seattle
Stefano Costanzi, National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Y. Vorobjev, Softberry, Inc.
N. Bakulina, Softberry, Inc.
V. Solovyev, Royal Holloway, University of London
Kazuhiko Kanou, Kitasato University
Daisuke Takaya, Kitasato University
Genki Terashi, Kitasato University
Mayuko Takeda-Shitaka, Kitasato University
Hideaki Umeyama, Kitasato University
William A. Goddard, California Institute of Technology
Youyong Li, California Institute of Technology
Soo Kyung Kim, California Institute of Technology

Document Type

Article

Publication Date

1-1-2009

Abstract

Recent breakthroughs in the determination of the crystal structures of G protein-coupled receptors (GPCRs) have provided new opportunities for structure-based drug design strategies targeting this protein family. With the aim of evaluating the current status of GPCR structure prediction and ligand docking, a community-wide, blind prediction assessment - GPCR Dock 2008 - was conducted in coordination with the publication of the crystal structure of the human adenosine A2Areceptor bound to the ligand ZM241385. Twenty-nine groups submitted 206 structural models before the release of the experimental structure, which were evaluated for the accuracy of the ligand binding mode and the overall receptor model compared with the crystal structure. This analysis highlights important aspects for success and future development, such as accurate modelling of structurally divergent regions and use of additional biochemical insight such as disulphide bridges in the extracellular loops.

Publication Source (Journal or Book title)

Nature Reviews Drug Discovery

First Page

455

Last Page

463

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