Please use this identifier to cite or link to this item: https://apo.ansto.gov.au/dspace/handle/10238/1855
Title: Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function
Authors: Whitten, AE
Jeffries, CM
Harris, SP
Trewhella, J
Keywords: Small angle scattering
Myosin
Muscles
Phosphorylation
Hypertrophy
Actin
Issue Date: 25-Nov-2008
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
URI: http://dx.doi.org/10.1073/pnas.0808903105
http://apo.ansto.gov.au/dspace/handle/10238/1855
ISSN: 0027-8424
Appears in Collections:Journal Articles

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