1rgp

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[[Image:1rgp.gif|left|200px]]
 
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==GTPASE-ACTIVATION DOMAIN FROM RHOGAP==
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The line below this paragraph, containing "STRUCTURE_1rgp", creates the "Structure Box" on the page.
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<StructureSection load='1rgp' size='340' side='right'caption='[[1rgp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rgp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1RGP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgp OCA], [https://pdbe.org/1rgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgp RCSB], [https://www.ebi.ac.uk/pdbsum/1rgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgp ProSAT]</span></td></tr>
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{{STRUCTURE_1rgp| PDB=1rgp | SCENE= }}
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</table>
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== Function ==
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'''GTPASE-ACTIVATION DOMAIN FROM RHOGAP'''
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rgp_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1RGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGP OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rgp ConSurf].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9009196 9009196]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Barrett, T.]]
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[[Category: Barrett T]]
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[[Category: Dodson, E J.]]
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[[Category: Dodson EJ]]
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[[Category: Dodson, G.]]
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[[Category: Dodson G]]
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[[Category: Eccleston, J F.]]
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[[Category: Eccleston JF]]
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[[Category: Gamblin, S J.]]
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[[Category: Gamblin SJ]]
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[[Category: Ludbrook, S B.]]
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[[Category: Ludbrook SB]]
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[[Category: Musacchio, A.]]
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[[Category: Musacchio A]]
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[[Category: Nurmahomed, K.]]
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[[Category: Nurmahomed K]]
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[[Category: Smerdon, S J.]]
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[[Category: Smerdon SJ]]
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[[Category: Xiao, B.]]
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[[Category: Xiao B]]
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[[Category: G-protein]]
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[[Category: Gap]]
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[[Category: Signal-transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:28:31 2008''
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Current revision

GTPASE-ACTIVATION DOMAIN FROM RHOGAP

PDB ID 1rgp

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