Rho GTPase activating protein

Function

Rho 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],^[2]. RhoGAPs contain a RhoGAP domain.

RhoGAP7 activates the small GTPases RHOA, RHOB, RHOC and CDC42.

Relevance

RhoGAPs are present in altered abundance in a variety of human cancers and may serve as targets for cancer therapy^[3].

Structural highlights

The contains a and GDP^[4]. Water molecules are shown as red spheres. .

3D structures of Rho GTPase activating protein

Rho GTPase activating protein 3D structures

Human RhoGAP 1 (magenta) complex with RhoA (blue), GDP, MgF3 and Mg+2 ions (PDB code 1ow3)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Moon SY, Zheng Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 2003 Jan;13(1):13-22. PMID:12480336
↑ Tcherkezian J, Lamarche-Vane N. Current knowledge of the large RhoGAP family of proteins. Biol Cell. 2007 Feb;99(2):67-86. doi: 10.1042/BC20060086. PMID:17222083 doi:http://dx.doi.org/10.1042/BC20060086
↑ 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

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Michal Harel, Joel L. Sussman, Alexander Berchansky

[1] Moon SY, Zheng Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 2003 Jan;13(1):13-22. PMID:12480336

[2] Tcherkezian J, Lamarche-Vane N. Current knowledge of the large RhoGAP family of proteins. Biol Cell. 2007 Feb;99(2):67-86. doi: 10.1042/BC20060086. PMID:17222083 doi:http://dx.doi.org/10.1042/BC20060086

[3] Kandpal RP. Rho GTPase activating proteins in cancer phenotypes. Curr Protein Pept Sci. 2006 Aug;7(4):355-65. PMID:16918449

[4] 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

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