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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 18360-18365 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 105 |
| Issue number | 47 |
| DOIs | |
| State | Published - Nov 25 2008 |
| Externally published | Yes |
Keywords
- C protein
- Familial hypertrophic cardiomypathy
- Muscle regulation
- Neutron contrast variation
- Small-angle scattering
ASJC Scopus subject areas
- General
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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. https://doi.org/10.1073/pnas.0808903105