Structure of the rgRGS domain of p115RhoGEF

Nat Struct Biol. 2001 Sep;8(9):805-9. doi: 10.1038/nsb0901-805.


p115RhoGEF, a guanine nucleotide exchange factor for Rho GTPase, is also a GTPase activating protein (GAP) for G(12) and G(13) heterotrimeric G alpha subunits. Near its N-terminus, p115RhoGEF contains a domain (rgRGS) with remote sequence identity to RGS (regulators of G protein signaling) domains. The rgRGS domain is necessary but not sufficient for the GAP activity of p115RhoGEF. The 1.9 A resolution crystal structure of the rgRGS domain shows structural similarity to RGS domains but possesses a C-terminal extension that folds into a layer of helices that pack against the hydrophobic core of the domain. Mutagenesis experiments show that rgRGS may form interactions with G alpha(13) that are analogous to those in complexes of RGS proteins with their G alpha substrates.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Guanine Nucleotide Exchange Factors / chemistry*
  • Guanine Nucleotide Exchange Factors / genetics
  • Guanine Nucleotide Exchange Factors / metabolism*
  • Heterotrimeric GTP-Binding Proteins / chemistry
  • Heterotrimeric GTP-Binding Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein Subunits
  • Rho Guanine Nucleotide Exchange Factors
  • Sequence Alignment


  • Guanine Nucleotide Exchange Factors
  • Peptide Fragments
  • Protein Subunits
  • Rho Guanine Nucleotide Exchange Factors
  • Heterotrimeric GTP-Binding Proteins

Associated data

  • PDB/1IAP