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PMID: 4033758 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Changing the binding specificity of a repressor by redesigning an alpha-helix.

Nature ·Vol. 316 ·No. 6029 ·1985-00-00 ·Pages 601-5

Wharton RP, Ptashne M

Abstract

We replaced amino acids on the 'outside', or solvent-exposed, surface of the DNA recognition alpha-helix of 434 repressor with the corresponding amino acids from the recognition helix of P22 repressor. The binding specificity of the resulting hybrid protein, as measured in vivo and in vitro, was that of P22 repressor.

MeSH Terms
Amino Acid Sequence Bacteriophages/genetics DNA, Viral/genetics Operon Protein Conformation Repressor Proteins Transcription Factors
Chemicals
DNA, Viral Repressor Proteins Transcription Factors
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wharton R P
Ptashne M
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/316601a0
Published
1985-00-00
Pages
601-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
NIGMS NIH HHS · GM 29109 · United States
External Links
PubMed source DOI: 10.1038/316601a0 View journal details
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