The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.

@article{Agou2004TheTD,
  title={The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.},
  author={Fabrice Agou and François Traincard and Emilie Vinolo and Gilles Courtois and Shoji Yamaoka and Alain Isra{\"e}l and M. Veron},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 27},
  pages={27861-9}
}
NEMO (NF-kappaB essential modulator) plays a key role in the canonical NF-kappaB pathway as the scaffold/regulatory component of the IkappaB kinase (IKK) complex. The self-association of NEMO involves the C-terminal halves of the polypeptide chains containing two putative coiled-coil motifs (a CC2 and a LZ leucine zipper), a proline-rich region, and a ZF zinc finger motif. Using purified truncation mutants, we showed that the minimal oligomerization domain of NEMO is the CC2-LZ segment and that… CONTINUE READING

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