doi: 10.1038/373311a0.
Structure of the NF-kappa B p50 homodimer bound to DNA
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- PMID: 7830764
- DOI: 10.1038/373311a0
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Structure of the NF-kappa B p50 homodimer bound to DNA
Nature.
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Abstract
The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-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 carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.
Comment in
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DNA-binding proteins. A butterfly flutters by.Nature. 1995 Jan 26;373(6512):287-8. doi: 10.1038/373287a0. Nature. 1995. PMID: 7830761 No abstract available.
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