Structural basis for self-association and receptor recognition of human TRAF2

Young Chul Park, Vicki Burkitt, Anthony R. Villa, Liang Tong and Hao Wu ()
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Young Chul Park: The Weill Medical College and Graduate School of Medical Sciences of Cornell University
Vicki Burkitt: The Weill Medical College and Graduate School of Medical Sciences of Cornell University
Anthony R. Villa: The Weill Medical College and Graduate School of Medical Sciences of Cornell University
Liang Tong: Columbia University
Hao Wu: The Weill Medical College and Graduate School of Medical Sciences of Cornell University

Nature, 1999, vol. 398, issue 6727, 533-538

Abstract: Abstract 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 receptor1. 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 domain2. 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 β-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.

Date: 1999
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DOI: 10.1038/19110

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