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1f3v
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1f3v.png|left|200px]] | ||
| - | + | ==Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2== | |
| - | + | <StructureSection load='1f3v' size='340' side='right'caption='[[1f3v]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |
| - | --> | + | <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> |
| - | + | <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> | |
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f3/1f3v_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[TNF receptor-associated factor|TNF receptor-associated factor]] | |
| - | + | *[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Hsia | + | [[Category: Large Structures]] |
| - | [[Category: Liou | + | [[Category: Hsia C]] |
| - | [[Category: Myszka | + | [[Category: Liou H-C]] |
| - | [[Category: Park | + | [[Category: Myszka D]] |
| - | [[Category: Rich | + | [[Category: Park YC]] |
| - | [[Category: Segal | + | [[Category: Rich R]] |
| - | [[Category: Wu | + | [[Category: Segal D]] |
| - | [[Category: Ye | + | [[Category: Wu H]] |
| - | + | [[Category: Ye H]] | |
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Current revision
Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2
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Categories: Homo sapiens | Large Structures | Hsia C | Liou H-C | Myszka D | Park YC | Rich R | Segal D | Wu H | Ye H

