Structure of the NF-κB p50 homodimer bound to DNA

@article{Mller1995StructureOT,
  title={Structure of the NF-κB p50 homodimer bound to DNA},
  author={Christoph W M{\"u}ller and F{\'e}lix A Rey and Mikiko Sodeoka and Gregory L. Verdine and Stephen C Harrison},
  journal={Nature},
  year={1995},
  volume={373},
  pages={311-317}
}
The structure of a large fragment of the p50 subunit of the human transcription factor NF-κB, bound as a homodimer to DNA, reveals that the Rel-homology region has two β-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the car boxy-terminal dimerization domain bears the site of I-κB interaction. The folds of these domains are related to immunoglobulin-like… CONTINUE READING

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