2pbi | pdb_00002pbi
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 GOL as ligand. Known structural/functional Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8 and AC9. 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
Page seeded by OCA on Thu Feb 21 18:27:54 2008
