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|Title:||Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function|
|Keywords:||Small angle scattering|
|Publisher:||National Academy of Sciences|
|Citation:||Whitten, A. E., Jeffries, C. M., Harris, S. P., & Trewhella, J. (2008). Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proceedings of the National Academy of Sciences of the United States of America, 105(47), 18360-18365. doi:10.1073/pnas.0808903105|
|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. © 2008, National Academy of Sciences|
|Gov't Doc #:||1398|
|Appears in Collections:||Journal Articles|
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