Rho GTPase activating protein: Difference between revisions
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<StructureSection load='1ow3' size='450' side='right' caption='Human RhoGAP 1 | <StructureSection load='1ow3' size='450' side='right' caption='Human RhoGAP 1 complex with RhoA , GDP, MgF3 and Mg+2 ions (PDB code [[1ow3]])' scene='75/750307/Cv/5' pspeed='8'> | ||
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== Function == | == Function == | ||
Revision as of 10:16, 30 April 2017
FunctionRho GTPase activating protein (RhoGAP) are one of the main classes of Rho GTPase regulators that are crucial in cell cytoskeletal organization, growth, differentiation, neuronal development and synaptic functions[1]. RhoGAPs contain a RhoGAP domain. RelevanceRhoGAPs are present in altered abundance in a variety of human cancers and may serve as targets for cancer therapy[2]. Structural highlightsThe contains a and GDP[3]. Water molecules shown as red spheres. .
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3D structures of Rho GTPase activating protein3D structures of Rho GTPase activating protein
Updated on 30-April-2017
4u3k - yRhoGAP 1 RhoGAP domain - yeast
1ow3 - hRhoGAP 1 residues 198-439 + RhoA + GDP - human
4wpc - yRhoGAP 1 F-BARR domain + inositol phosphate
4rtt, 4rug, 2gnc - hRhoGAP 2 SLIT-ROBO SH3 domain
2dl8 - hRhoGAP 2 SLIT-ROBO SH3 domain - NMR
2epd - hRhoGAP 4 SH3 domain - NMR
2ee4 , 2ee5 - hRhoGAP 5 (mutant) RhoGAP domain - NMR
3kuq - hRhoGAP 7 RhoGAP domain
2kap, 2dky - hRhoGAP 7 SAM domain - NMR
2p0d, 2p0f, 2p0h - hRhoGAP 9 pleckstrin homology domain + phosphoinositide
2mio - hRhoGAP 10 SH3 domain - NMR
2j59 - hRhoGAP 10 ARF-binding domain + ADP-ribosylation factor
3eap - hRhoGAP 11A RhoGAP domain
3byi - RhoGAP 15 residues 262-473
3msx - hRhoGAP 20 RhoGAP domain + RhoA
2yuy - hRhoGAP 21 PDZ domain - NMR
2dhj - hRhoGAP 21 pleckstrin homology domain - NMR
3pp2 - hRhoGAP 27 pleckstrin homology domain
5irc - RhoGAP 35 + RhoA - rat
1grn - hRhoGAP C-terminal + GTP-binding protein
ReferencesReferences
- ↑ Moon SY, Zheng Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 2003 Jan;13(1):13-22. PMID:12480336
- ↑ Kandpal RP. Rho GTPase activating proteins in cancer phenotypes. Curr Protein Pept Sci. 2006 Aug;7(4):355-65. PMID:16918449
- ↑ Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF. MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81. PMID:11927263