Crystal structure of the multifunctional Gβ5–RGS9 complex | Zendy

Matthew L. Cheever | Zendy; Jason T. Snyder | Zendy; Svetlana Gershburg | Zendy; David P. Siderovski | Zendy; T. Kendall Harden | Zendy; John Sondek | Zendy

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Crystal 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.

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