期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 47, 页码 18360-18365出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0808903105
关键词
familial hypertrophic cardiomypathy; C protein; muscle regulation; neutron contrast variation; small-angle scattering
资金
- Australian Research Council Federation Fellowship [FF0457488]
- U.S. Department of Energy [DE-FG02-05ER64026]
- National Institutes of Health [HL080367]
- National Science Foundation [DMR-0454672]
- Australian government's Access to Major Research Facilities Program [06/07-N-27]
- Australian Institute of Nuclear Science and Engineering [AINGRA062S7]
- Australian Research Council [FF0457488] Funding Source: Australian Research Council
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.
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