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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1995 Nov 7;92(23):10644–10647. doi: 10.1073/pnas.92.23.10644

Target sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin.

A Houdusse 1, C Cohen 1
PMCID: PMC40668  PMID: 7479857

Abstract

Some of the rules for how members of the calmodulin (CaM) superfamily bind to target peptides are revealed by the crystal structure of the regulatory domain of scallop myosin. The structure shows that the IQ motif of the heavy chain in this invertebrate myosin imposes constraints on both the positioning and conformation of the individual lobes of the light chains. In contrast, analysis of the contact residues in the targets bound by Ca(2+)-CaM reveals how the structure of CaM accommodates a broader range of sequences consonant with this protein's functional diversity.

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Selected References

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