1ca9: Difference between revisions

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[[Image:1ca9.png|left|200px]]


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==STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2==
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<StructureSection load='1ca9' size='340' side='right'caption='[[1ca9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ca9]] is a 8 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=1CA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CA9 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]] 2.3&#8491;</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=1ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca9 OCA], [https://pdbe.org/1ca9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ca9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ca9 ProSAT]</span></td></tr>
{{STRUCTURE_1ca9|  PDB=1ca9  |  SCENE=  }}
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== Function ==
[https://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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/1ca9_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=1ca9 ConSurf].
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== Publication Abstract from PubMed ==
Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily and the interleukin-1 receptor. They are important in the regulation of cell survival and cell death. The carboxy-terminal region of TRAFs (the TRAF domain) is required for self-association and interaction with receptors. The domain contains a predicted coiled-coil region that is followed by a highly conserved TRAF-C domain. Here we report the crystal structure of the TRAF domain of human TRAF2, both alone and in complex with a peptide from TNF receptor-2 (TNF-R2). The structures reveal a trimeric self-association of the TRAF domain, which we confirm by studies in solution. The TRAF-C domain forms a new, eight-stranded antiparallel beta-sandwich structure. The TNF-R2 peptide binds to a conserved shallow surface depression on one TRAF-C domain and does not contact the other protomers of the trimer. The nature of the interaction indicates that an SXXE motif may be a TRAF2-binding consensus sequence. The trimeric structure of the TRAF domain provides an avidity-based explanation for the dependence of TRAF recruitment on the oligomerization of the receptors by their trimeric extracellular ligands.


===STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2===
Structural basis for self-association and receptor recognition of human TRAF2.,Park YC, Burkitt V, Villa AR, Tong L, Wu H Nature. 1999 Apr 8;398(6727):533-8. PMID:10206649<ref>PMID:10206649</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10206649 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_10206649}}
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</StructureSection>
==About this Structure==
1CA9 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=1CA9 OCA].
 
==Reference==
Structural basis for self-association and receptor recognition of human TRAF2., Park YC, Burkitt V, Villa AR, Tong L, Wu H, Nature. 1999 Apr 8;398(6727):533-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10206649 10206649]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Burkitt, V.]]
[[Category: Burkitt V]]
[[Category: Park, Y C.]]
[[Category: Park YC]]
[[Category: Tong, L.]]
[[Category: Tong L]]
[[Category: Villa, A R.]]
[[Category: Villa AR]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: Adapter protein]]
[[Category: Cell survival]]
[[Category: Tnf signaling]]
[[Category: Traf]]
 
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