2rgn

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 2rgn, resolution 3.500Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA

Overview

The guanine nucleotide exchange factor p63RhoGEF is an effector of the, heterotrimeric guanine nucleotide-binding protein (G protein) Galphaq and, thereby links Galphaq-coupled receptors (GPCRs) to the activation of the, small-molecular-weight G protein RhoA. We determined the crystal structure, of the Galphaq-p63RhoGEF-RhoA complex, detailing the interactions of, Galphaq with the Dbl and pleckstrin homology (DH and PH) domains of, p63RhoGEF. These interactions involve the effector-binding site and the, C-terminal region of Galphaq and appear to relieve autoinhibition of the, catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown, to constitute a family of Galphaq effectors that appear to activate RhoA, both in vitro and in intact cells. We propose that this structure, represents the crux of an ancient signal transduction pathway that is, expected to be important in an array of physiological processes.

About this Structure

2RGN is a Protein complex structure of sequences from Homo sapiens and Mus musculus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs., Lutz S, Shankaranarayanan A, Coco C, Ridilla M, Nance MR, Vettel C, Baltus D, Evelyn CR, Neubig RR, Wieland T, Tesmer JJ, Science. 2007 Dec 21;318(5858):1923-7. PMID:18096806

Page seeded by OCA on Wed Jan 23 11:09:07 2008