Rho GTPase
From Proteopedia
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| - | <StructureSection load='1tx4' size='340' side='right' caption=' | + | <StructureSection load='1tx4' size='340' side='right' caption='Human RhoA (green) complex with RhoGAP (grey), GDP, AlF4 and Mg+2 ion (green) (PDB code [[1tx4]])' scene=''> |
== Function == | == Function == | ||
| - | '''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''' and '''RhoC'''. These 3 proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>. | + | '''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''' and '''RhoC'''. These 3 proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>. |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | + | The transition state complex of RhoA and RhoGAP contains GDP, AlF4 and Mg+2 ion<ref>PMID:9338791</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 10:36, 8 February 2017
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3D structures of Rho GTPase
Updated on 08-February-2017
References
- ↑ Sepp KJ, Auld VJ. RhoA and Rac1 GTPases mediate the dynamic rearrangement of actin in peripheral glia. Development. 2003 May;130(9):1825-35. PMID:12642488
- ↑ Zhou J, Hayakawa Y, Wang TC, Bass AJ. RhoA mutations identified in diffuse gastric cancer. Cancer Cell. 2014 Jul 14;26(1):9-11. doi: 10.1016/j.ccr.2014.06.022. PMID:25026207 doi:http://dx.doi.org/10.1016/j.ccr.2014.06.022
- ↑ Jin L, Burnett AL. RhoA/Rho-kinase in erectile tissue: mechanisms of disease and therapeutic insights. Clin Sci (Lond). 2006 Feb;110(2):153-65. PMID:16411892 doi:http://dx.doi.org/10.1042/CS20050255
- ↑ Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ. Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature. 1997 Oct 16;389(6652):758-62. PMID:9338791 doi:10.1038/39651
