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Calcium-Dependent Interaction Occurs between Slow Skeletal Myosin Binding Protein C and Calmodulin

Department of Microbiology, Miami University, Oxford, OH 45056, USA
Cell, Molecular, and Structural Biology Program, Miami University, Oxford, OH 45056, USA
Department of Cardiology, Johns Hopkins University, Baltimore, MD 21205, USA
Department of Internal Medicine, Heart Branch of the Heart, Lung and Vascular Institute, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA
Author to whom correspondence should be addressed.
Present affiliation Department of Biophysics, Medical College of Wisconsin, 8701 W. Watertown Plank Road, Milwaukee, WI 2042, USA.
Magnetochemistry 2018, 4(1), 1;
Received: 1 November 2017 / Revised: 12 December 2017 / Accepted: 15 December 2017 / Published: 21 December 2017
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy)
PDF [3150 KB, uploaded 22 December 2017]


Myosin binding protein C (MyBP-C) is a multi-domain protein that participates in the regulation of muscle contraction through dynamic interactions with actin and myosin. Three primary isoforms of MyBP-C exist: cardiac (cMyBP-C), fast skeletal (fsMyBP-C), and slow skeletal (ssMyBP-C). The N-terminal region of cMyBP-C contains the M-motif, a three-helix bundle that binds Ca2+-loaded calmodulin (CaM), but less is known about N-terminal ssMyBP-C and fsMyBP-C. Here, we characterized the conformation of a recombinant N-terminal fragment of ssMyBP-C (ssC1C2) using differential scanning fluorimetry, nuclear magnetic resonance, and molecular modeling. Our studies revealed that ssC1C2 has altered thermal stability in the presence and absence of CaM. We observed that site-specific interaction between CaM and the M-motif of ssC1C2 occurs in a Ca2+-dependent manner. Molecular modeling supported that the M-motif of ssC1C2 likely adopts a three-helix bundle fold comparable to cMyBP-C. Our study provides evidence that ssMyBP-C has overlapping structural determinants, in common with the cardiac isoform, which are important in controlling protein–protein interactions. We shed light on the differential molecular regulation of contractility that exists between skeletal and cardiac muscle. View Full-Text
Keywords: calcium; calmodulin; molecular model; MyBP-C; NMR; protein calcium; calmodulin; molecular model; MyBP-C; NMR; protein

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Springer, T.I.; Johns, C.W.; Cable, J.; Lin, B.L.; Sadayappan, S.; Finley, N.L. Calcium-Dependent Interaction Occurs between Slow Skeletal Myosin Binding Protein C and Calmodulin. Magnetochemistry 2018, 4, 1.

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