TNF receptor-associated factor
FunctionTNF receptor-associated factor (TRAF) are signal transducers and are involved in regulation of apoptosis, inflammation and antiviral response. There are 7 known TRAF proteins. All TRAF proteins share a C-terminal homology region named TRAF domain which can bind the cytoplasmic domain of receptors and other TRAF proteins[1]. TRAF1 is the only TRAF which does not have N-terminal RING and zinc finger motifs. TRAF2, TRAF5 and TRAF6 mediate activation of NF-κB and JNK. TRAF3 mediates some innate immune receptor signals and regulates some post-translational modifications[2]. TRAF4 is a binding partner of glycoproteins in platelets[3]. Structural highlightsThe interaction of TRAF2 with the adaptor protein TRADD is bipartite with one part containing mainly hydrophobic interactions while the second part contains mainly polar interactions[4].
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3D Structures of TNF receptor-associated factor
Updated on 15-September-2016
- TRAF1
- 3m0d – hTRAF1 residues 266-329 + hTRAF2 + cIAP2 - human
- 3m0d – hTRAF1 residues 266-329 + hTRAF2 + cIAP2 - human
- TRAF2
- TRAF2 complex with peptide
- 1ca9 – hTRAF2 TRAF domain + TNF-R2 peptide
- 1qsc, 1d00, 1czz – hTRAF2 TRAF domain + CD40 receptor peptide
- 1d01 – hTRAF2 TRAF domain + CD30 peptide
- 1czy – hTRAF2 TRAF domain + latent membrane protein peptide
- 1d0a – hTRAF2 TRAF domain + OX40L receptor peptide
- 1d0j – hTRAF2 TRAF domain + 4-1BB ligand receptor peptide
- 1f3v – hTRAF2 TRAF domain + TRADD N terminal
- 3m0a – hTRAF2 residues 266-329 + cIAP2
- 1ca9 – hTRAF2 TRAF domain + TNF-R2 peptide
- TRAF3
- 4ghu – TRAF3 TRAF domain residues 376-567 + antiviral-signaling protein peptide - mouse
- 4ghu – TRAF3 TRAF domain residues 376-567 + antiviral-signaling protein peptide - mouse
- TRAF4
- TRAF5
- 4gjh – hTRAF5 TRAF domain residues 381-558
- 4gjh – hTRAF5 TRAF domain residues 381-558
- TRAF6
- TRAF6 complex with peptide