1ca9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ca9]] is a 8 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=1CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CA9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ca9]] is a 8 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=1CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CA9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ca9 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ca9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Burkitt, V | [[Category: Burkitt, V]] | ||
[[Category: Park, Y C | [[Category: Park, Y C]] | ||
[[Category: Tong, L | [[Category: Tong, L]] | ||
[[Category: Villa, A R | [[Category: Villa, A R]] | ||
[[Category: Wu, H | [[Category: Wu, H]] | ||
[[Category: Adapter protein]] | [[Category: Adapter protein]] | ||
[[Category: Cell survival]] | [[Category: Cell survival]] | ||
[[Category: Tnf signaling]] | [[Category: Tnf signaling]] | ||
[[Category: Traf]] | [[Category: Traf]] | ||
Revision as of 12:44, 22 December 2014
STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTumour 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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