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The Calmodulin-Binding Domain of Caldesmon Binds to Calmodulin in an .alpha.-Helical Conformation
The binding of calcium+almodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. It has been reported that a 17-residue synthetic peptide encompassing the residues Gly651-Ser667 of smooth muscle CaD constitutes its CaM-binding domain [Zhan, Q., Wong, S. S., & Wang, C. L. A. (1991) J. Biol. Chem. 266, 21810-218141. This peptide does not share sequence homology with the CaM-binding domains of other proteins, and in addition, the binding of C a M to CaD isdoi:10.1021/bi00171a016 pmid:8110748 fatcat:dpai336jsnfw3iuclqlvw4octq