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. 1995 Jan 26;373(6512):303-10.
doi: 10.1038/373303a0.

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

G Ghosh  1 , G van Duyne, S Ghosh, P B Sigler
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Structure of NF-kappa B p50 homodimer bound to a kappa B site

G Ghosh et al. Nature. .

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.

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