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Nature. 1995 Jan 26;373(6512):303-10.

Structure of NF-kappa B p50 homodimer bound to a kappa B site.

Author information

1
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.

Abstract

The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.

PMID:
7530332
DOI:
10.1038/373303a0
[Indexed for MEDLINE]

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