2fnf

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[[Image:2fnf.png|left|200px]]
 
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{{STRUCTURE_2fnf| PDB=2fnf | SCENE= }}
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==C1 domain of Nore1==
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<StructureSection load='2fnf' size='340' side='right'caption='[[2fnf]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FNF 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">Solution NMR</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=ZN:ZINC+ION'>ZN</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=2fnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnf OCA], [https://pdbe.org/2fnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fnf RCSB], [https://www.ebi.ac.uk/pdbsum/2fnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fnf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RASF5_MOUSE RASF5_MOUSE] Potental tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing (By similarity). May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS1 and KRAS induced apoptosis.<ref>PMID:11864565</ref>
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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/fn/2fnf_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=2fnf 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 novel Ras effector mNore1, capable of inducing apoptosis, is a multidomain protein. It comprises a C1 domain homologous to PKC and an RA domain similar to the Ras effectors AF-6 and RalGDS. Here, we determine the affinity of these two domains to the active forms of Ras and Rap1 using isothermal calorimetric titration. The interaction of Ras/Rap1-GTP with the RA domain of mNore1 is weakened significantly by direct binding of the C1 domain to the RA domain. In order to analyze this observation in atomic detail, we solved the C1 solution structure by NMR. By determining chemical shifts and relaxation rates, we can show an intramolecular complex of C1-RA. GTP-Ras titration and binding to RA disrupts this complex and displaces the C1 domain. Once the C1 domain tumbles freely in solution, a lipid binding interface becomes accessible. Furthermore, we provide evidence of phosphatidylinositol 3-phosphate binding of the free C1 domain.
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===C1 domain of Nore1===
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GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1.,Harjes E, Harjes S, Wohlgemuth S, Muller KH, Krieger E, Herrmann C, Bayer P Structure. 2006 May;14(5):881-8. PMID:16698549<ref>PMID:16698549</ref>
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{{ABSTRACT_PUBMED_16698549}}
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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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==About this Structure==
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<div class="pdbe-citations 2fnf" style="background-color:#fffaf0;"></div>
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[[2fnf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNF OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016698549</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Bayer, P.]]
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[[Category: Bayer P]]
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[[Category: Harjes, E.]]
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[[Category: Harjes E]]
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[[Category: Harjes, S.]]
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[[Category: Harjes S]]
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[[Category: Herrmann, C.]]
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[[Category: Herrmann C]]
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[[Category: Krieger, E.]]
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[[Category: Krieger E]]
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[[Category: Muller, K H.]]
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[[Category: Muller KH]]
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[[Category: Wohlgemuth, S.]]
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[[Category: Wohlgemuth S]]
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[[Category: Apoptosis]]
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[[Category: Cysteine rich domain]]
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[[Category: Signal transduction]]
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[[Category: Zinc]]
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Current revision

C1 domain of Nore1

PDB ID 2fnf

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