1NFK

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

(1995) Nature 373: 303-310

• PubMed: 7530332 Search on PubMed
• DOI: https://doi.org/10.1038/373303a0
• Primary Citation of Related Structures:  
  1NFK


• PubMed 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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Organizational Affiliation: 

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