2RGN: Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA

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.
PDB ID: 2RGNDownload
MMDB ID: 61823
PDB Deposition Date: 2007/10/4
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 2RGN: trimeric; determined by author and by software (PISA)
Molecular Components in 2RGN
Label Count Molecule
Proteins (3 molecules)
Guanine Nucleotide-binding Protein G(i) Subunit Alpha-1,guanine Nucleotide-binding Protein G(q) Subunit Alpha(Gene symbol: Gnai1)
Molecule annotation
RHO Guanine Nucleotide Exchange Factor 25(Gene symbol: ARHGEF25)
Molecule annotation
Transforming Protein Rhoa(Gene symbol: RHOA)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB