Structure of the rgRGs domain of p115RhoGEF

Authors

Zhe Chen, University of Texas Southwestern Medical Center
Clark D. Wells, University of Texas Southwestern Medical Center
Paul C. Sternweis, University of Texas Southwestern Medical Center
Stephen R. Sprang, University of Montana

Document Type

Article

Publication Title

Nature Structural Biology

Publication Date

9-2001

Volume

8

Issue

9

Disciplines

Biology | Life Sciences

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.

DOI

https://doi.org/10.1038/nsb0901-805

Rights

© 2001 Nature Publishing Group

Recommended Citation

Chen, Zhe; Wells, Clark D.; Sternweis, Paul C.; and Sprang, Stephen R., "Structure of the rgRGs domain of p115RhoGEF" (2001). Biological Sciences Faculty Publications. 522.
https://scholarworks.umt.edu/biosci_pubs/522