Recognition of DNA sequences by the repressor of bacteriophage 434

S. C. Harrison*, J. E. Anderson, G. B. Koudelka, A. Mondragon, S. Subbiah, R. P. Wharton, C. Wolberger, M. Ptashne

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The structure of a complex between the DNA-binding domain of phase 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important far sequence-specific recognition A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide -NH groups and DNA phosphates, position the repressor and fix the DNA configurations. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.

Original languageEnglish (US)
Pages (from-to)31-37
Number of pages7
JournalBiophysical Chemistry
Issue number1-2
StatePublished - Feb 1988


  • DNA sequence recognition
  • DNA-protein binding
  • Repressor-operator complex
  • Transcriptional regulation
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry


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