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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Young Chul Park & Vicki Burkitt & Anthony R. Villa & Liang Tong & Hao Wu, 1999. "Structural basis for self-association and receptor recognition of human TRAF2," Nature, Nature, vol. 398(6727), pages 533-538, April.
  • Handle: RePEc:nat:nature:v:398:y:1999:i:6727:d:10.1038_19110
    DOI: 10.1038/19110
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    Cited by:

    1. Fabian Giehler & Michael S. Ostertag & Thomas Sommermann & Daniel Weidl & Kai R. Sterz & Helmut Kutz & Andreas Moosmann & Stephan M. Feller & Arie Geerlof & Brigitte Biesinger & Grzegorz M. Popowicz &, 2024. "Epstein-Barr virus-driven B cell lymphoma mediated by a direct LMP1-TRAF6 complex," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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