1azt
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(New page: 200px<br /><applet load="1azt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azt, resolution 2.3Å" /> '''GS-ALPHA COMPLEXED WI...)
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Revision as of 09:07, 20 November 2007
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GS-ALPHA COMPLEXED WITH GTP-GAMMA-S
Overview
The crystal structure of Gsalpha, the heterotrimeric G protein alpha, subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a, complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is, the prototypic member of a family of GTP-binding proteins that regulate, the activities of effectors in a hormone-dependent manner. Comparison of, the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests, that their effector specificity is primarily dictated by the shape of the, binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein, signaling to stimulate the GTPase activity of Gsalpha. The betagamma, binding surface of Gsalpha is largely conserved in sequence and structure, to that of Gialpha, whereas differences in the surface formed by the, carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor, specificity.
About this Structure
1AZT is a Single protein structure of sequence from Bos taurus with MG, PO4 and GSP as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the adenylyl cyclase activator Gsalpha., Sunahara RK, Tesmer JJ, Gilman AG, Sprang SR, Science. 1997 Dec 12;278(5345):1943-7. PMID:9395396
Page seeded by OCA on Tue Nov 20 11:14:23 2007
