Ras GTPase activating protein
From Proteopedia
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== Function == | == Function == | ||
[[Ras GTPase activating protein]] (RasGAP) inactivates Ras from its active GTP-bound form to its GDP-bound form<ref>PMID:9113414</ref>. It is part of the mitogenic signal transmission via its N-terminal SH2-SH3-SH2 domains. | [[Ras GTPase activating protein]] (RasGAP) inactivates Ras from its active GTP-bound form to its GDP-bound form<ref>PMID:9113414</ref>. It is part of the mitogenic signal transmission via its N-terminal SH2-SH3-SH2 domains. | ||
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== Relevance == | == Relevance == | ||
Inactivated RasGAP activate RAS which is mutated in 30% of cancer types<ref>PMID:24814062</ref>. RasGAP Colra1 is involved in infection-related morphogenesis in gourd family plants<ref>PMID:25275394</ref>. | Inactivated RasGAP activate RAS which is mutated in 30% of cancer types<ref>PMID:24814062</ref>. RasGAP Colra1 is involved in infection-related morphogenesis in gourd family plants<ref>PMID:25275394</ref>. | ||
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== 3D Structures of Ras GTPase activating protein == | == 3D Structures of Ras GTPase activating protein == | ||
Revision as of 10:48, 22 January 2017
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3D Structures of Ras GTPase activating protein
Updated on 22-January-2017
2gqi, 2m51 – hRasGAP SH3 domain – human – NMR
2j05, 2j06, 4fss - hRasGAP SH3 domain
2gsb - hRasGAP SH2 domain – NMR
3bxj - hRasGAP SYNGAP fragment - rat
References
- ↑ Tocque B, Delumeau I, Parker F, Maurier F, Multon MC, Schweighoffer F. Ras-GTPase activating protein (GAP): a putative effector for Ras. Cell Signal. 1997 Feb;9(2):153-8. PMID:9113414
- ↑ Maertens O, Cichowski K. An expanding role for RAS GTPase activating proteins (RAS GAPs) in cancer. Adv Biol Regul. 2014 May;55:1-14. doi: 10.1016/j.jbior.2014.04.002. Epub 2014 Apr, 30. PMID:24814062 doi:http://dx.doi.org/10.1016/j.jbior.2014.04.002
- ↑ Harata K, Kubo Y. Ras GTPase activating protein CoIra1 is involved in infection-related morphogenesis by regulating cAMP and MAPK signaling pathways through CoRas2 in Colletotrichum orbiculare. PLoS One. 2014 Oct 2;9(9):e109045. doi: 10.1371/journal.pone.0109045. eCollection, 2014. PMID:25275394 doi:http://dx.doi.org/10.1371/journal.pone.0109045

