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Comparison of two different DMA-binding modes of the NF-κB p50 homodimer

Nature Structural Biology volume 3, pages 224–227 (1996)Cite this article

Abstract

Analysis of the NF-κB p50 homodimer bound to different DNA sequences shows that the protein can recognize half-site spacings of either three or four base pairs. The protein can maintain most of its DNA contacts by a relative reorientation of its two domains.

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Author notes

  1. Christoph W. Müller

    Present address: EMBL, Grenoble Outstation, c/o lLL BP156, F-38042, Grenoble, CEDEX 9, France

  2. Félix A. Rey

    Present address: Laboratoire de Biologie Structural, CNRS - Bat. 34,1, Ave. de la Terrasse, 91198, Gif-sur-Yvette Cedex, France

Authors and Affiliations

  1. Howard Hughes Medical Institute and Harvard University Department of Molecular and Cellular Biology, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

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

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  1. Christoph W. Müller
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  2. Félix A. Rey
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Müller, C., Rey, F. & Harrison, S. Comparison of two different DMA-binding modes of the NF-κB p50 homodimer. Nat Struct Mol Biol 3, 224–227 (1996). https://doi.org/10.1038/nsb0396-224

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