Rho GTPase activating protein
From Proteopedia
(Difference between revisions)
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The <scene name='75/750307/Cv/6'>active site of RhoGAP</scene> contains a <scene name='75/750307/Cv/7'>catalytic arginine</scene> and GDP<ref>PMID:11927263</ref>. Water molecules are shown as red spheres. <scene name='75/750307/Cv/8'>Mg/MgF3 coordination site</scene>. | The <scene name='75/750307/Cv/6'>active site of RhoGAP</scene> contains a <scene name='75/750307/Cv/7'>catalytic arginine</scene> and GDP<ref>PMID:11927263</ref>. Water molecules are shown as red spheres. <scene name='75/750307/Cv/8'>Mg/MgF3 coordination site</scene>. | ||
| + | ==3D structures of Rho GTPase activating protein== | ||
| + | [[Rho GTPase activating protein 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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*RhoGAP 1 | *RhoGAP 1 | ||
| - | **[[5my3]] - yRhoGAP 1 RhoGAP domain - yeast<br /> | ||
**[[1ow3]], [[5m6x]], [[5m70]] - hRhoGAP 1 residues 198-439 + RhoA + GDP - human<br /> | **[[1ow3]], [[5m6x]], [[5m70]] - hRhoGAP 1 residues 198-439 + RhoA + GDP - human<br /> | ||
| + | **[[6r3v]] - hRhoGAP 1 GTPase-activating domain residues 1-439 + RhoA + GDP + Pi<br /> | ||
**[[4wpc]] - yRhoGAP 1 F-BARR domain + inositol phosphate<br /> | **[[4wpc]] - yRhoGAP 1 F-BARR domain + inositol phosphate<br /> | ||
| + | **[[5my3]] - yRhoGAP 1 RhoGAP domain - yeast<br /> | ||
*RhoGAP 2 | *RhoGAP 2 | ||
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**[[3eap]] - hRhoGAP 11A RhoGAP domain<br /> | **[[3eap]] - hRhoGAP 11A RhoGAP domain<br /> | ||
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| + | * RhoGAP 12 | ||
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| + | **[[6gvc]] - hRhoGAP 12 residues 683-837 + actin + ATP<br /> | ||
*RhoGAP 15 | *RhoGAP 15 | ||
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**[[5irc]] - RhoGAP 35 + RhoA - rat<br /> | **[[5irc]] - RhoGAP 35 + RhoA - rat<br /> | ||
| + | **[[6d4g]] - rRhoGAP 35 + GTP<br /> | ||
*RhoGAP | *RhoGAP | ||
Revision as of 07:22, 16 December 2019
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3D structures of Rho GTPase activating protein
Updated on 16-December-2019
References
- ↑ 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
