Function 
TNF 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 highlights 
The interaction of TRAF2 with the adaptor protein TRADD is [4]. Hydrophobic,  Polar
  3D Structures of TNF receptor-associated factor 
TNF receptor-associated factor 3D structures