Trends Biochem Sci. 1990 Feb;15(2):59-64.

How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices.

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E. I. du Pont de Nemours & Co., Central Research and Development Department, Wilmington, DE 19880-0328.

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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