2rgn
From Proteopedia
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|PDB= 2rgn |SIZE=350|CAPTION= <scene name='initialview01'>2rgn</scene>, resolution 3.500Å | |PDB= 2rgn |SIZE=350|CAPTION= <scene name='initialview01'>2rgn</scene>, resolution 3.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5 | + | |LIGAND= <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Gnaq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), GEFT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RHOA, ARH12, ARHA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= Gnaq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), GEFT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RHOA, ARH12, ARHA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:49:27 2008'' |
Revision as of 13:49, 23 March 2008
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| , resolution 3.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | Gnaq (Mus musculus), GEFT (Homo sapiens), RHOA, ARH12, ARHA, RHO12 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 23 15:49:27 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Nance, M R. | Shankaranarayanan, A. | Tesmer, J J.G. | ALF | GDP | MG | Adp-ribosylation | Cytoplasm | Cytoskeleton | Galpha-q | Galphaq | Gq | Gtp-binding | Heterotrimeric g-protein | Lipoprotein | Magnesium | Membrane | Methylation | Nucleotide-binding | P63rhogef | Palmitate | Prenylation | Protein-protein complex | Proto-oncogene | Rhoa | Rhogef | Signaling complex | Signaling protein complex | Small molecular weight g-protein | Transducer
