1gua

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(New page: 200px<br /> <applet load="1gua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gua, resolution 2.0&Aring;" /> '''HUMAN RAP1A, RESIDUE...)
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[[Image:1gua.gif|left|200px]]<br />
 
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<applet load="1gua" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gua, resolution 2.0&Aring;" />
 
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'''HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131'''<br />
 
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==Overview==
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==HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131==
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Members of the Ras subfamily of small GTP-binding proteins have been shown, to be promiscuous towards a variety of putative effector molecules such as, the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange, factor (Ral-GEF). To address the question of specificity of interactions, we have introduced the mutations E30D and K31E into Rap and show, biochemically, by X-ray structure analysis and by transfection in vivo, that the identical core effector region of Ras and Rap (residues 32-40) is, responsible for molecular recognition, but that residues outside this, region are responsible for the specificity of the interaction. The major, determinant for the switch in specificity is the opposite charge of, residue 31--Lys in Rap, Glu in Ras--which creates a favourable, complementary interface for the Ras-Raf interaction.
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<StructureSection load='1gua' size='340' side='right'caption='[[1gua]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gua]] is a 2 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=1GUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GUA 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&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1gua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gua OCA], [https://pdbe.org/1gua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gua RCSB], [https://www.ebi.ac.uk/pdbsum/1gua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gua ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RAP1A_HUMAN RAP1A_HUMAN] Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner.
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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/gu/1gua_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=1gua ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1GUA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, CA and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUA OCA].
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Ras/Rap effector specificity determined by charge reversal., Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A, Nat Struct Biol. 1996 Aug;3(8):723-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8756332 8756332]
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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: Nassar, N.]]
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[[Category: Nassar N]]
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[[Category: Wittinghofer, A.]]
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[[Category: Wittinghofer A]]
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[[Category: CA]]
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[[Category: GNP]]
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[[Category: MG]]
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[[Category: complex (gtp-binding/atp-binding)]]
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[[Category: oncogene protein/kinase/effector protein gtp-binding-protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:09:07 2007''
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Current revision

HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131

PDB ID 1gua

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