The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits.

@article{Huang1997TheRO,
  title={The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits.},
  author={D B Huang and T. J. Huxford and Yelin Chen and Gourisankar Ghosh},
  journal={Structure},
  year={1997},
  volume={5 11},
  pages={1427-36}
}
BACKGROUND Members of the rel/NFkappaB family of transcription factors play a vital role in the regulation of rapid cellular responses, such as those required to fight infection or react to cellular stress. Members of this family of proteins form homo- and heterodimers with differing affinities for dimerization. They share a structural motif known as the rel homology region (RHR), the C-terminal one third of which mediates protein dimerization. Crystal structures of the rel/NFkappaB family… CONTINUE READING
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