1srq

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[[Image:1srq.gif|left|200px]]
 
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==Crystal Structure of the Rap1GAP catalytic domain==
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The line below this paragraph, containing "STRUCTURE_1srq", creates the "Structure Box" on the page.
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<StructureSection load='1srq' size='340' side='right'caption='[[1srq]], [[Resolution|resolution]] 2.90&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'>[[1srq]] is a 4 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=1SRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SRQ FirstGlance]. <br>
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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]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1srq| PDB=1srq | SCENE= }}
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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=1srq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srq OCA], [https://pdbe.org/1srq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1srq RCSB], [https://www.ebi.ac.uk/pdbsum/1srq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1srq ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of the Rap1GAP catalytic domain'''
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== Function ==
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[https://www.uniprot.org/uniprot/RPGP1_HUMAN RPGP1_HUMAN] GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Rap1 is a Ras-like guanine-nucleotide-binding protein (GNBP) that is involved in a variety of signal-transduction processes. It regulates integrin-mediated cell adhesion and might activate extracellular signal-regulated kinase. Like other Ras-like GNBPs, Rap1 is regulated by guanine-nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs). These GAPs increase the slow intrinsic GTPase reaction of Ras-like GNBPs by many orders of magnitude and allow tight regulation of signalling. The activation mechanism involves stabilization of the catalytic glutamine of the GNBP and, in most cases, the insertion of a catalytic arginine of GAP into the active site. Rap1 is a close homologue of Ras but does not possess the catalytic glutamine essential for GTP hydrolysis in all other Ras-like and Galpha proteins. Furthermore, RapGAPs are not related to other GAPs and apparently do not use a catalytic arginine residue. Here we present the crystal structure of the catalytic domain of the Rap1-specific Rap1GAP at 2.9 A. By mutational analysis, fluorescence titration and stopped-flow kinetic assay, we demonstrate that Rap1GAP provides a catalytic asparagine to stimulate GTP hydrolysis. Implications for the disease tuberous sclerosis are discussed.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1srq_consurf.spt"</scriptWhenChecked>
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1SRQ 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=1SRQ OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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The GTPase-activating protein Rap1GAP uses a catalytic asparagine., Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A, Nature. 2004 May 13;429(6988):197-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15141215 15141215]
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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=1srq ConSurf].
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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: Chakrabarti, P P.]]
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[[Category: Chakrabarti PP]]
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[[Category: Daumke, O.]]
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[[Category: Daumke O]]
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[[Category: Vetter, I R.]]
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[[Category: Vetter IR]]
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[[Category: Weyand, M.]]
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[[Category: Weyand M]]
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[[Category: Wittinghofer, A.]]
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[[Category: Wittinghofer A]]
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[[Category: Mixed alpha-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:04:10 2008''
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Current revision

Crystal Structure of the Rap1GAP catalytic domain

PDB ID 1srq

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