2pbi

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2pbi, resolution 1.950Å

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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 Feb;15(2):155-62. Epub 2008 Jan 20. PMID:18204463

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