1f3v

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[[Image:1f3v.gif|left|200px]]
 
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==Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2==
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The line below this paragraph, containing "STRUCTURE_1f3v", creates the "Structure Box" on the page.
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<StructureSection load='1f3v' size='340' side='right'caption='[[1f3v]], [[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'>[[1f3v]] 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=1F3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3V 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1f3v| PDB=1f3v | 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=1f3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3v OCA], [https://pdbe.org/1f3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3v RCSB], [https://www.ebi.ac.uk/pdbsum/1f3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRADD_HUMAN TRADD_HUMAN] The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B.
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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/f3/1f3v_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=1f3v ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF TRADD AND THE TRAF DOMAIN OF TRAF2'''
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==See Also==
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*[[TNF receptor-associated factor|TNF receptor-associated factor]]
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*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
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==Overview==
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__TOC__
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TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure of the TRADD-TRAF2 complex, which is highly distinct from receptor-TRAF2 interactions. This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF2 signaling is more readily initiated by TRADD than by direct receptor-TRAF2 interactions. TRADD is specific for TRAF1 and TRAF2, which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex. The stronger affinity and unique specificity of the TRADD-TRAF2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction.
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</StructureSection>
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==About this Structure==
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1F3V 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=1F3V OCA].
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==Reference==
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A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction., Park YC, Ye H, Hsia C, Segal D, Rich RL, Liou HC, Myszka DG, Wu H, Cell. 2000 Jun 23;101(7):777-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10892748 10892748]
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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: Hsia, C.]]
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[[Category: Hsia C]]
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[[Category: Liou, H C.]]
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[[Category: Liou H-C]]
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[[Category: Myszka, D.]]
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[[Category: Myszka D]]
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[[Category: Park, Y C.]]
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[[Category: Park YC]]
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[[Category: Rich, R.]]
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[[Category: Rich R]]
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[[Category: Segal, D.]]
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[[Category: Segal D]]
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[[Category: Wu, H.]]
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[[Category: Wu H]]
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[[Category: Ye, H.]]
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[[Category: Ye H]]
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[[Category: A-b sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:51:38 2008''
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Current revision

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2

PDB ID 1f3v

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