1SHZ

Crystal Structure of the p115RhoGEF rgRGS Domain in A Complex with Galpha(13):Galpha(i1) Chimera

Summary for 1SHZ

• Entry DOI: 10.2210/pdb1shz/pdb
• Related: 1AGR 1AZS 1FQJ 1IAP
• Descriptor: Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera, Rho guanine nucleotide exchange factor 1, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: signal transduction, protein complex, signaling protein
• Biological source: Rattus norvegicus (house mouse, Norway rat); More
• Cellular location: Nucleus: P10824; Cytoplasm : Q92888
• Total number of polymer chains: 4
• Total formula weight: 133115.10

Authors

Chen, Z.,Singer, W.D.,Sternweis, P.C.,Sprang, S.R. (deposition date: 2004-02-26, release date: 2005-01-18, Last modification date: 2023-08-23)

Primary citation

Chen, Z.,Singer, W.D.,Sternweis, P.C.,Sprang, S.R.
Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator.
Nat.Struct.Mol.Biol., 12:191-197, 2005

PubMed Abstract: p115RhoGEF, a guanine nucleotide exchange factor (GEF) for Rho GTPase, is also a GTPase-activating protein (GAP) for G12 and G13 heterotrimeric Galpha subunits. The GAP function of p115RhoGEF resides within the N-terminal region of p115RhoGEF (the rgRGS domain), which includes a module that is structurally similar to RGS (regulators of G-protein signaling) domains. We present here the crystal structure of the rgRGS domain of p115RhoGEF in complex with a chimera of Galpha13 and Galphai1. Two distinct surfaces of rgRGS interact with Galpha. The N-terminal betaN-alphaN hairpin of rgRGS, rather than its RGS module, forms intimate contacts with the catalytic site of Galpha. The interface between the RGS module of rgRGS and Galpha is similar to that of a Galpha-effector complex, suggesting a role for the rgRGS domain in the stimulation of the GEF activity of p115RhoGEF by Galpha13.

PubMed: 15665872
DOI: 10.1038/nsmb888

Experimental method

X-RAY DIFFRACTION (2.85 Å)