Figure 3

Overall structure of TRAF7 CC region. (A) Schematic diagram showing the domain organization of TRAF7: a RING domain, a ZF domain, a CC domain, and seven WD40 repeats. (B) Ribbon diagram representation of the TRAF7 CC crystal. The crystal was obtained using TRAF7 fragment 270–379 aa, and prominent electronic cloud density was observed in residues E285–L377. TRAF7 CC forms a parallel trimer, presented here with three chains in green, magenta, and cyan. (C) MALS measurement of TRAF7 CC (fragment 270–379 aa) and TRAF7 ZF-CC (fragment 221–379 aa) showing that the measured molecular weights align with trimeric TRAF7 in solution. Theoretical molecular weights of the trimers: TRAF7 CC, 42.3 kDa; TRAF7 ZF-CC, 59.1 kDa. (D) Sequence alignment of human TRAF CC regions across paralogs, revealing low sequence similarity between human TRAF7 CC and human TRAF1–6 CC. The letters a–g below the TRAF7 sequence are the residue positions of the heptad repeats in the CC region. (E) Sequence alignment of TRAF7 CC regions across species, demonstrating high sequence identity in human, rat, chicken, frog, and zebrafish.