2RGN

Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA

Summary for 2RGN

• Entry DOI: 10.2210/pdb2rgn/pdb
• Related: 2bcj
• Descriptor: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha, Rho guanine nucleotide exchange factor 25, Transforming protein RhoA, ... (7 entities in total)
• Functional Keywords: heterotrimeric g-protein, small molecular weight g-protein, signaling complex, protein-protein complex, rhogef, rhoa, galphaq, galpha-q, p63rhogef, gq, gtp-binding, lipoprotein, nucleotide-binding, palmitate, transducer, adp-ribosylation, cytoskeleton, magnesium, membrane, methylation, prenylation, proto-oncogene, signaling protein complex
• Biological source: Rattus norvegicus (Rat); More
• Cellular location: Cell membrane : Q86VW2; Cell membrane; Lipid-anchor; Cytoplasmic side: P61586
• Total number of polymer chains: 6
• Total formula weight: 209214.51

Authors

Shankaranarayanan, A.,Nance, M.R.,Tesmer, J.J.G. (deposition date: 2007-10-04, release date: 2008-01-15, Last modification date: 2023-08-30)

Primary citation

Lutz, S.,Shankaranarayanan, A.,Coco, C.,Ridilla, M.,Nance, M.R.,Vettel, C.,Baltus, D.,Evelyn, C.R.,Neubig, R.R.,Wieland, T.,Tesmer, J.J.
Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs.
Science, 318:1923-1927, 2007

PubMed Abstract: 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.

PubMed: 18096806
DOI: 10.1126/science.1147554

Experimental method

X-RAY DIFFRACTION (3.5 Å)