1tx4: Difference between revisions

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[[Category: transition state]]
[[Category: transition state]]


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Revision as of 17:01, 30 October 2007

File:1tx4.gif


1tx4, resolution 1.65Å

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RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX

OverviewOverview

Small G proteins of the Rho family, which includes Rho, Rac and Cdc42Hs, regulate phosphorylation pathways that control a range of biological, functions including cytoskeleton formation and cell proliferation. They, operate as molecular switches, cycling between the biologically active, GTP-bound form and the inactive GDP-bound state. Their rate of hydrolysis, of GTP to GDP by virtue of their intrinsic GTPase activity is slow, but, can be accelerated by up to 10(5)-fold through interaction with rhoGAP, a, GTPase-activating protein that stimulates Rho-family proteins. As such, rhoGAP plays a crucial role in regulating Rho-mediated signalling, pathways. Here we report the crystal structure of RhoA and rhoGAP, complexed with the transition-state analogue GDP.AlF4- at 1.65 A, resolution. ... [(full description)]

About this StructureAbout this Structure

1TX4 is a [Protein complex] structure of sequences from [Homo sapiens] with MG, ALF and GDP as [ligands]. Structure known Active Site: TS. Full crystallographic information is available from [OCA].

ReferenceReference

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue., Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ, Nature. 1997 Oct 16;389(6652):758-62. PMID:9338791

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