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Structure of NF-κB p50 homodimer bound to a κB site

Nature volume 373, pages 303–310 (1995)Cite this article

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.

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Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, 295 Congress Avenue, New Haven, Connecticut, 06510, USA

    Gourisankar Ghosh, Gregory Van Duyne, Sankar Ghosh & Paul B. Sigler

  2. Section of Immunobiology, Yale University, 295 Congress Avenue, New Haven, Connecticut, 06510, USA

    Sankar Ghosh

Authors
  1. Gourisankar Ghosh
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  2. Gregory Van Duyne
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  3. Sankar Ghosh
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  4. Paul B. Sigler
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Ghosh, G., Duyne, G., Ghosh, S. et al. Structure of NF-κB p50 homodimer bound to a κB site. Nature 373, 303–310 (1995). https://doi.org/10.1038/373303a0

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