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spinqualitylabelsall models 1ca4, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2)

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

1CA4 is a Single protein structure of sequence 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

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