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Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DMA-binding domain bound to its DNA target

Nature volume 359, pages 505–512 (1992)Cite this article

Abstract

The dominant transcriptional regulator of the papiIlomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric ant i para I lei β-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed α-helices. The specific interface is an 'interwoven' network of interactions where the identifying base pairs of the target contact more than one amino-acid side chain and the discriminating amino acids interact with more than one base pair.

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Author information

Author notes

  1. Steven R. Grossman

    Present address: Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts, 02115, USA

Authors and Affiliations

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

    Rashmi S. Hegde & Paul B. Sigler

  2. Department of Molecular Genetics and Cell Biology and the Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, 60637, USA

    Steven R. Grossman & Laimonis A. Laimins

Authors
  1. Rashmi S. Hegde
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  2. Steven R. Grossman
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  3. Laimonis A. Laimins
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  4. Paul B. Sigler
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Hegde, R., Grossman, S., Laimins, L. et al. Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DMA-binding domain bound to its DNA target. Nature 359, 505–512 (1992). https://doi.org/10.1038/359505a0

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