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Structure of the NF-κB p50 homodimer bound to DNA

Nature volume 373, pages 311–317 (1995)Cite this article

Abstract

The structure of a large fragment of the p50 subunit of the human transcription factor NF-κB, bound as a homodimer to DNA, reveals that the Rel-homology region has two β-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the car boxy-terminal dimerization domain bears the site of I-κB interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.

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Authors and Affiliations

  1. Howard Hughes Medical Institute, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Christoph W. Müller & Stephen C. Harrison

  2. Harvard University Department of Molecular and Cellular Biology, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Christoph W. Müller, Félix A. Rey & Stephen C. Harrison

  3. Harvard University Department of Chemistry, 12 Oxford Street, Cambridge, Massachusetts, 02138, USA

    Mikiko Sodeoka & Gregory L. Verdine

  4. University of Tokyo, Faculty of Pharmaceutical Sciences, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113, Japan

    Mikiko Sodeoka

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Müller, C., Rey, F., Sodeoka, M. et al. Structure of the NF-κB p50 homodimer bound to DNA. Nature 373, 311–317 (1995). https://doi.org/10.1038/373311a0

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