Open AccessCrystal structure of the multifunctional Gβ5–RGS9 complex
Author(s) -
Matthew L. Cheever,
Jason T. Snyder,
Svetlana Gershburg,
David P. Siderovski,
T. Kendall Harden,
John Sondek
Publication year - 2008
Publication title -
nature structural and molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.448
H-Index - 270
eISSN - 1545-9993
pISSN - 1545-9985
DOI - 10.1038/nsmb.1377
Subject(s) - g protein , g protein coupled receptor , protein subunit , gtpase activating protein , microbiology and biotechnology , regulator of g protein signaling , gtpase , signal transduction , biology , gq alpha subunit , chemistry , biochemistry , gene
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.