1rgp

<table><tr><td colspan='2'>[[1rgp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RGP FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgp OCA], [http://pdbe.org/1rgp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rgp RCSB], [http://www.ebi.ac.uk/pdbsum/1rgp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgp ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.

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== Publication Abstract from PubMed ==

Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP. The structure is an unusual arrangement of nine alpha-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity.

The structure of the GTPase-activating domain from p50rhoGAP.,Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K, Gamblin SJ, Musacchio A, Smerdon SJ, Eccleston JF Nature. 1997 Jan 30;385(6615):458-61. PMID:9009196<ref>PMID:9009196</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Barrett, T]]

[[Category: Dodson, E J]]

[[Category: Dodson, G]]

[[Category: Eccleston, J F]]

[[Category: Gamblin, S J]]

[[Category: Ludbrook, S B]]

[[Category: Musacchio, A]]

[[Category: Nurmahomed, K]]

[[Category: Smerdon, S J]]

[[Category: Xiao, B]]

[[Category: Signal-transduction]]