Structure of the rgRGs domain of p115RhoGEF

Zhe Chen, Clark Wells, Paul C. Sternweis, Stephen R. Sprang

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

p115RhoGEF, a guanine nucleotide exchange factor for Rho GTPase, is also a GTPase activating protein (GAP) for G12 and G13 heterotrimeric Gα 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 Å 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 Gα13 that are analogous to those in complexes of RGS proteins with their Gα substrates.

Original languageEnglish (US)
Pages (from-to)805-809
Number of pages5
JournalNature Structural Biology
Volume8
Issue number9
DOIs
StatePublished - 2001
Externally publishedYes

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Rho Guanine Nucleotide Exchange Factors
GTP-Binding Protein Regulators
GTPase-Activating Proteins
GTP-Binding Proteins
RGS Proteins
Guanine Nucleotide Exchange Factors
rho GTP-Binding Proteins
Mutagenesis
Nucleotides
Crystal structure
Experiments
Protein Domains

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Structure of the rgRGs domain of p115RhoGEF. / Chen, Zhe; Wells, Clark; Sternweis, Paul C.; Sprang, Stephen R.

In: Nature Structural Biology, Vol. 8, No. 9, 2001, p. 805-809.

Research output: Contribution to journalArticle

Chen, Z, Wells, C, Sternweis, PC & Sprang, SR 2001, 'Structure of the rgRGs domain of p115RhoGEF', Nature Structural Biology, vol. 8, no. 9, pp. 805-809. https://doi.org/10.1038/nsb0901-805
Chen, Zhe ; Wells, Clark ; Sternweis, Paul C. ; Sprang, Stephen R. / Structure of the rgRGs domain of p115RhoGEF. In: Nature Structural Biology. 2001 ; Vol. 8, No. 9. pp. 805-809.
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