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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.]] | ||
[[Category: | [[Category: Adapter protein]] | ||
[[Category: | [[Category: Cell survival]] | ||
[[Category: | [[Category: Tnf signaling]] | ||
[[Category: | [[Category: Traf]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:31:21 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:31, 2 May 2008
STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2
OverviewOverview
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 StructureAbout this Structure
1CA9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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