Abstract
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 modules. The amino-terminal domain also resembles the core domain of p53.
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Müller, C., Rey, F., Sodeoka, M. et al. Structure of the NF-κB p50 homodimer bound to DNA. Nature 373, 311–317 (1995). https://doi.org/10.1038/373311a0
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DOI: https://doi.org/10.1038/373311a0
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