Structure of the NF-κB p50 homodimer bound to DNA View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-01

AUTHORS

C W Müller, F A Rey, M Sodeoka, G L Verdine, S C Harrison

ABSTRACT

The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-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 carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53. More... »

PAGES

311-317

Journal

TITLE

Nature

ISSUE

6512

VOLUME

373

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/373311a0

    DOI

    http://dx.doi.org/10.1038/373311a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1026631071

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7830764


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