Figure 4
From: Structural analysis of TIFA: Insight into TIFA-dependent signal transduction in innate immunity

Structural insights into TIFA–TRAF6 oligomeric complex. (A) Model of a TIFA oligomeric complex for binding to TRAF6-C, based on the TIFA hexamer, in combination with the phosphorylation-dependent head-to-tail interactions15. A minor change of the hexameric form enables head-to-tail interactions; the resulting TIFA oligomeric complex has three faces for TRAF6-C binding (red arrows at bottom right). (B) Interactions between TIFA oligomeric complex and TRAF6-Cs viewed from one face. TRAF6-C is shown in green and the TIFA peptide including TRAF6-binding motif is shown in magenta. Red and magenta spheres indicate the Cα atoms of Leu149 of TIFA and the N-terminal Ser174 of the TRAF6-binding motif of TIFA, respectively.