1ca9

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[[Image:1ca9.gif|left|200px]]
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{{Structure
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1ca9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB]</span>
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'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2'''
'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2'''
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[[Category: Villa, A R.]]
[[Category: Villa, A R.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
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[[Category: adapter protein]]
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[[Category: Adapter protein]]
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[[Category: cell survival]]
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[[Category: Cell survival]]
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[[Category: tnf signaling]]
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[[Category: Tnf signaling]]
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[[Category: traf]]
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[[Category: Traf]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:31:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:46 2008''
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Revision as of 09:31, 2 May 2008

Image:1ca9.gif

Template:STRUCTURE 1ca9

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2


Overview

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.

About this Structure

1CA9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from 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:10206649 Page seeded by OCA on Fri May 2 12:31:21 2008

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