The molecular basis of DNA-protein recognition inferred from the structure of cro repressor

Nature. 1982 Aug 19;298(5876):718-23. doi: 10.1038/298718a0.

Abstract

Recognition by cro repressor protein of its specific DNA binding sites appears to occur via multidentate hydrogen bonds between amino acid side chains of the protein and base-pair atoms in the major groove of right-handed B-form DNA. Most of the sequence-specific interactions between cro and DNA, as well as a number of sequence-independent ones, are mediated by a two-alpha-helical unit which appears to be common to many proteins that regulate gene expression.

Publication types

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

MeSH terms

  • Bacteriophage lambda / genetics
  • Base Sequence
  • Carrier Proteins / metabolism*
  • DNA / metabolism*
  • DNA-Binding Proteins
  • Escherichia coli / genetics*
  • Hydrogen Bonding
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Conformation
  • Repressor Proteins / metabolism*
  • Structure-Activity Relationship
  • Transcription Factors / metabolism*
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • Repressor Proteins
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins
  • DNA