Summary
PDB 1CA9 deposited: 1999-02-25 modified: 2009-02-24
Title STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2
Authors Burkitt, V., Park, Y.C., Tong, L., Villa, A.R., Wu, H.
Method X-RAY DIFFRACTION
Structure factors resolution 2.3 rfactor 0.234 rfree 0.289
DPI 0.66 theoretical min: 0.33
Related PDB Entries 1CA4
Citations

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.

Nature. 1999 Apr 8;398(6727):533-8.

Cross References
Database source Identifier Description
PubMed 10206649 NATUAS
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1CA9/1 1CA9 1 pentamer 0 5 2 4557
1CA9/2 1CA9 2 trimer 0 3 0 4284
1CA9/3 1CA9 3 octamer 0 8 2 8846