1f3v: Difference between revisions

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-{{STRUCTURE_1f3v|  PDB=1f3v  |  SCENE=  }}
-===Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2===
-{{ABSTRACT_PUBMED_10892748}}
-==Function==
+==Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2==
-[[http://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. [[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref>
+<StructureSection load='1f3v' size='340' side='right'caption='[[1f3v]], [[Resolution|resolution]] 2.00&Aring;' 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]] 2&#8491;</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>
-==About this Structure==
+==See Also==
-[[1f3v]] is a 2 chain structure with sequence 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].
+*[[TNF receptor-associated factor|TNF receptor-associated factor]]
+*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
-==Reference==
+__TOC__
-<ref group="xtra">PMID:010892748</ref><references group="xtra"/><references/>
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Hsia, C.]]
+[[Category: Large Structures]]
-[[Category: Liou, H C.]]
+[[Category: Hsia C]]
-[[Category: Myszka, D.]]
+[[Category: Liou H-C]]
-[[Category: Park, Y C.]]
+[[Category: Myszka D]]
-[[Category: Rich, R.]]
+[[Category: Park YC]]
-[[Category: Segal, D.]]
+[[Category: Rich R]]
-[[Category: Wu, H.]]
+[[Category: Segal D]]
-[[Category: Ye, H.]]
+[[Category: Wu H]]
-[[Category: A-b sandwich]]
+[[Category: Ye H]]
-[[Category: Apoptosis]]