How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices.
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.
O'Neil
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E. I. du Pont de Nemours & Co., Central Research and Development Department, Wilmington, DE 19880-0328.
DeGrado
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D000595:Amino Acid Sequence; D002147:Calmodulin / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D008715:Methionine