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Nature. 1995 Jan 26;373(6512):311-7.

Structure of the NF-kappa B p50 homodimer bound to DNA.

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  • 1Howard Hughes Medical Institute, Cambridge, Massachusetts 02138.


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.

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