2pbi
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(New page: 200px<br /><applet load="2pbi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pbi, resolution 1.950Å" /> '''The multifunctional...)
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Revision as of 08:58, 31 January 2008
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The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure
Overview
Regulators of G-protein signaling (RGS) proteins enhance the intrinsic, GTPase activity of G protein alpha (Galpha) subunits and are vital for, proper signaling kinetics downstream of G protein-coupled receptors, (GPCRs). R7 subfamily RGS proteins specifically and obligately dimerize, with the atypical G protein beta5 (Gbeta5) subunit through an internal G, protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the, 1.95-A crystal structure of the Gbeta5-RGS9 complex, which is essential, for normal visual and neuronal signal transduction. This structure reveals, a canonical RGS domain that is functionally integrated within a molecular, complex that is poised for integration of multiple steps during G-protein, activation and deactivation.
About this Structure
2PBI is a Protein complex structure of sequences from Mus musculus with as ligand. Known structural/functional Sites: , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of the multifunctional Gbeta5-RGS9 complex., Cheever ML, Snyder JT, Gershburg S, Siderovski DP, Harden TK, Sondek J, Nat Struct Mol Biol. 2008 Jan 20;. PMID:18204463
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