Structure of NF-kappa B p50 homodimer bound to a kappa B site - PubMed (original) (raw)
. 1995 Jan 26;373(6512):303-10.
doi: 10.1038/373303a0.
Affiliations
- PMID: 7530332
- DOI: 10.1038/373303a0
Structure of NF-kappa B p50 homodimer bound to a kappa B site
G Ghosh et al. Nature. 1995.
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.
Comment in
- DNA-binding proteins. A butterfly flutters by.
Baltimore D, Beg AA. Baltimore D, et al. Nature. 1995 Jan 26;373(6512):287-8. doi: 10.1038/373287a0. Nature. 1995. PMID: 7830761 No abstract available.
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