Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors.

ABSTRACT: G protein-coupled receptors with seven transmembrane alpha-helices (GPCRs) comprise the largest receptor superfamily and are involved in detecting a wide variety of extracellular stimuli. The availability of high-resolution crystal structures of five prototypical GPCRs, bovine and squid rhodopsin, engineered A(2A)-adenosine, beta(1)- and beta(2)-adrenergic receptors, permits comparative analysis of features common to these and likely all GPCRs. We provide an analysis of the distribution of water molecules in the transmembrane region of these GPCR structures and find conserved contacts with microdomains demonstrated to be involved in receptor activation. Colocalization of water molecules associating with highly conserved and functionally important residues in several of these GPCR crystal s

SUBMITTER: Angel TE 

PROVIDER: S-EPMC2688986 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature