Prediction of 3-d structure of the cro protein from phage 434

Miroslaw Cygler*, Wayne F. Anderson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

A comparative model building process has been utilized to predict the three-dimensional structure of the bacteriophage 434 Cro protein. Amino acid sequence similarities between the 434 Cro protein and other bacteriophage repressor and Cro proteins have been used, in conjunction with secondary structure prediction and the known structures of other base sequence specific DNA binding proteins, to derive the model. From this model the interactions between the 434 Cro protein and its operator DNA have been deduced. These proposed interactions are consistent with the known properties of the bacteriophage 434 Cro protein.

Original languageEnglish (US)
Pages (from-to)1055-1067
Number of pages13
JournalJournal of Biomolecular Structure and Dynamics
Volume3
Issue number6
DOIs
StatePublished - Jun 1986

Funding

We thank Dr. M. Ptashne for information on the 434 repressor amino terminal domain prior to its publication and Dr. C.O. Pabo for providing us with the coordinates of the N-terminal domain of .\. repressor. We acknowledge the computer programming assistance of Eric Harley. This work was supported by the Medical Research Council of Canada through the Group on Protein Structure and Function.

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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