3brw

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[[Image:3brw.jpg|left|200px]]
 
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{{Structure
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==Structure of the Rap-RapGAP complex==
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|PDB= 3brw |SIZE=350|CAPTION= <scene name='initialview01'>3brw</scene>, resolution 3.40&Aring;
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<StructureSection load='3brw' size='340' side='right'caption='[[3brw]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+D+172'>AC1</scene>, <scene name='pdbsite=AC2:Bef+Binding+Site+For+Residue+D+170'>AC2</scene> and <scene name='pdbsite=AC3:Gdp+Binding+Site+For+Residue+D+171'>AC3</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[3brw]] 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=3BRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BRW FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.4&#8491;</td></tr>
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|GENE= RAP1GAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RAP1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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|DOMAIN=
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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=3brw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3brw OCA], [https://pdbe.org/3brw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3brw RCSB], [https://www.ebi.ac.uk/pdbsum/3brw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3brw ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1srq|1SRQ]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3brw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3brw OCA], [http://www.ebi.ac.uk/pdbsum/3brw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3brw RCSB]</span>
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== Function ==
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}}
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/3brw_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=3brw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The GTP-binding protein Rap1 regulates integrin-mediated and other cell adhesion processes. Unlike most other Ras-related proteins, it contains a threonine in switch II instead of a glutamine (Gln61 in Ras), a residue crucial for the GTPase reaction of most G proteins. Furthermore, unlike most other GTPase-activating proteins (GAPs) for small G proteins, which supply a catalytically important Arg-finger, no arginine residue of RapGAP makes a significant contribution to the GTPase reaction of Rap1. For a detailed understanding of the reaction mechanism, we have solved the structure of Rap1 in complex with Rap1GAP. It shows that the Thr61 of Rap is away from the active site and that an invariant asparagine of RapGAPs, the Asn-thumb, takes over the role of the cis-glutamine of Ras, Rho or Ran. The structure and biochemical data allow to further explain the mechanism and to define the important role of a conserved tyrosine. The structure and biochemical data furthermore show that the RapGAP homologous region of the tumour suppressor Tuberin is sufficient for catalysis on Rheb.
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'''Structure of the Rap-RapGAP complex'''
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The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues.,Scrima A, Thomas C, Deaconescu D, Wittinghofer A EMBO J. 2008 Apr 9;27(7):1145-53. Epub 2008 Feb 28. PMID:18309292<ref>PMID:18309292</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3brw" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The GTP-binding protein Rap1 regulates integrin-mediated and other cell adhesion processes. Unlike most other Ras-related proteins, it contains a threonine in switch II instead of a glutamine (Gln61 in Ras), a residue crucial for the GTPase reaction of most G proteins. Furthermore, unlike most other GTPase-activating proteins (GAPs) for small G proteins, which supply a catalytically important Arg-finger, no arginine residue of RapGAP makes a significant contribution to the GTPase reaction of Rap1. For a detailed understanding of the reaction mechanism, we have solved the structure of Rap1 in complex with Rap1GAP. It shows that the Thr61 of Rap is away from the active site and that an invariant asparagine of RapGAPs, the Asn-thumb, takes over the role of the cis-glutamine of Ras, Rho or Ran. The structure and biochemical data allow to further explain the mechanism and to define the important role of a conserved tyrosine. The structure and biochemical data furthermore show that the RapGAP homologous region of the tumour suppressor Tuberin is sufficient for catalysis on Rheb.
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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3BRW is a [[Protein complex]] structure of sequences 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=3BRW OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues., Scrima A, Thomas C, Deaconescu D, Wittinghofer A, EMBO J. 2008 Feb 28;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18309292 18309292]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Deaconescu, D.]]
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[[Category: Deaconescu D]]
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[[Category: Scrima, A.]]
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[[Category: Scrima A]]
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[[Category: Thomas, C.]]
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[[Category: Thomas C]]
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[[Category: Wittinghofer, A.]]
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[[Category: Wittinghofer A]]
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[[Category: g protein]]
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[[Category: gap]]
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[[Category: gtp binding protein]]
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[[Category: gtp-binding]]
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[[Category: gtpase]]
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[[Category: gtpase activation]]
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[[Category: rap]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:32 2008''
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Current revision

Structure of the Rap-RapGAP complex

PDB ID 3brw

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