| First Author | Whitten AE | Year | 2008 |
| Journal | Proc Natl Acad Sci U S A | Volume | 105 |
| Issue | 47 | Pages | 18360-5 |
| PubMed ID | 19011110 | Mgi Jnum | J:248264 |
| Mgi Id | MGI:6093140 | Doi | 10.1073/pnas.0808903105 |
| Citation | Whitten AE, et al. (2008) Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proc Natl Acad Sci U S A 105(47):18360-5 |
| abstractText | 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. |
