Structure of NF-κB p50 homodimer bound to a κB site
- 26 January 1995
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 373 (6512) , 303-310
- https://doi.org/10.1038/373303a0
Abstract
The 2.3-Â crystal structure of the transcription factor NF-κB p50 homodimer bound to a palindromic κB 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 κB recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between β-sheets using residues that are strongly conserved in the Rel family.Keywords
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