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GPCR agonist binding revealed by modeling and crystallography

Summary: GPCR agonist binding revealed by
modeling and crystallography
Vsevolod Katritch*
and Ruben Abagyan
Skaggs School of Pharmacy and Pharmaceutical Sciences and San Diego Supercomputer Center, University of California,
San Diego, La Jolla, CA 92093, USA
Despite recent progress in structural coverage of the
G-protein-coupled receptor (GPCR) family, high plastici-
ty of these membrane proteins poses additional chal-
lenges for crystallographic studies of their complexes
with different classes of ligands, especially agonists. The
ability to predict computationally the binding of natural
and clinically relevant agonists and corresponding
changes in the receptor pocket, starting from inactive
GPCR structures, is therefore of great interest for under-
standing GPCR biology and drug action. Comparison of
computational models published in 2009 and 2010 with
recently determined agonist-bound structures of b-ad-
renergic and adenosine A2A receptors reveals high accu-
racy of the predicted agonist binding poses (0.8 A and


Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego


Collections: Biology and Medicine