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

Nature. 1992 Oct 8;359(6395):505-12. doi: 10.1038/359505a0.

Abstract

The dominant transcriptional regulator of the papillomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric antiparallel beta-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed alpha-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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Bovine papillomavirus 1 / genetics*
  • Crystallization
  • DNA / chemistry
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Hydrogen Bonding
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Nucleic Acid Conformation
  • Protein Folding
  • Viral Proteins / chemistry*
  • Viral Proteins / metabolism

Substances

  • DNA-Binding Proteins
  • E2 protein, Bovine papillomavirus
  • Macromolecular Substances
  • Viral Proteins
  • DNA