Crystal structure of the multifunctional Gbeta5-RGS9 complex

Nat Struct Mol Biol. 2008 Feb;15(2):155-62. doi: 10.1038/nsmb.1377. Epub 2008 Jan 20.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Dimerization
  • GTP-Binding Protein beta Subunits / chemistry*
  • Humans
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • RGS Proteins / chemistry*


  • GNB5 protein, human
  • GTP-Binding Protein beta Subunits
  • RGS Proteins
  • regulator of g-protein signaling 9

Associated data

  • PDB/2PBI