Interactions between cro repressor and the model specific binding site
- 1 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 175 (2), 317-320
- https://doi.org/10.1016/0014-5793(84)80759-0
Abstract
Binding of λ phage cro repressor to the synthetic half of OR3, the most conservative half of the specific binding sites, was investigated by proton nuclear magnetic resonance spectroscopy. It was found that the α-helical segment (27–36) of the protein was involved in specific interactions with the model binding site. The 3-dimensional structure of cro repressor does not change noticeably upon complex formation. Intercalation can be excluded as a possible means of interactionKeywords
This publication has 16 references indexed in Scilit:
- 1H NMR sudy of the interaction of bacteriophageλ Cro protein with the OR3 operator. Evidence for a change of the conformation of the OR3 operator on bindingNucleic Acids Research, 1984
- Comparison of the structures of Cro and λ repressor proteins from bacteriophage λJournal of Molecular Biology, 1983
- Studies of the structure of bacteriophage λ cro protein in solutionFEBS Letters, 1982
- Studies of the structure of bacteriophage λ cro protein in solutionFEBS Letters, 1982
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- λ Repressor and cro—components of an efficient molecular switchNature, 1981
- Structure of the cro repressor from bacteriophage λ and its interaction with DNANature, 1981
- A study of the efficiency and the problem of sulfonation of several condensing reagents and their mechanisms for the chemical synthesis of deoxyoligoribonucleotidesNucleic Acids Research, 1980
- How the λ repressor and cro workCell, 1980
- Autoregulation and Function of a Repressor in Bacteriophage LambdaScience, 1976