Review
doi: 10.1016/0968-0004(90)90177-d.
How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices
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- PMID: 2186516
- DOI: 10.1016/0968-0004(90)90177-d
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Review
How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices
Trends Biochem Sci.
1990 Feb.
Abstract
Calmodulin (CaM) is a protein capable of recognizing positively charged, amphiphilic alpha-helical peptides independent of their precise amino acid sequences; this structural feature has also been found in many CaM-binding proteins. Recent work involving crystallography and site-directed mutagenesis of CaM along with studies of photoreactive and fluorescent CaM-binding peptides have helped define how calmodulin interacts with amphiphilic helices.
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