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Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function.


ABSTRACT: Cardiac myosin-binding protein C (cMyBP-C) is an accessory protein of striated muscle sarcomeres that is vital for maintaining regular heart function. Its 4 N-terminal regulatory domains, C0-C1-m-C2 (C0C2), influence actin and myosin interactions, the basic contractile proteins of muscle. Using neutron contrast variation data, we have determined that C0C2 forms a repeating assembly with filamentous actin, where the C0 and C1 domains of C0C2 attach near the DNase I-binding loop and subdomain 1 of adjacent actin monomers. Direct interactions between the N terminus of cMyBP-C and actin thereby provide a mechanism to modulate the contractile cycle by affecting the regulatory state of the thin filament and its ability to interact with myosin.

SUBMITTER: Whitten AE 

PROVIDER: S-EPMC2587536 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function.

Whitten Andrew E AE   Jeffries Cy M CM   Harris Samantha P SP   Trewhella Jill J  

Proceedings of the National Academy of Sciences of the United States of America 20081114 47


Cardiac myosin-binding protein C (cMyBP-C) is an accessory protein of striated muscle sarcomeres that is vital for maintaining regular heart function. Its 4 N-terminal regulatory domains, C0-C1-m-C2 (C0C2), influence actin and myosin interactions, the basic contractile proteins of muscle. Using neutron contrast variation data, we have determined that C0C2 forms a repeating assembly with filamentous actin, where the C0 and C1 domains of C0C2 attach near the DNase I-binding loop and subdomain 1 of  ...[more]

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