Next Article in Journal / Special Issue
Accelerating NMR-Based Structural Studies of Proteins by Combining Amino Acid Selective Unlabeling and Fast NMR Methods
Previous Article in Journal / Special Issue
Local and Average Structural Changes in Zeolite A upon Ion Exchange
Article Menu
Issue 1 (March) cover image

Export Article

Open AccessArticle
Magnetochemistry 2018, 4(1), 1; doi:10.3390/magnetochemistry4010001

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

1
Department of Microbiology, Miami University, Oxford, OH 45056, USA
2
Cell, Molecular, and Structural Biology Program, Miami University, Oxford, OH 45056, USA
3
Department of Cardiology, Johns Hopkins University, Baltimore, MD 21205, USA
4
Department of Internal Medicine, Heart Branch of the Heart, Lung and Vascular Institute, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA
Present affiliation Department of Biophysics, Medical College of Wisconsin, 8701 W. Watertown Plank Road, Milwaukee, WI 2042, USA.
*
Author to whom correspondence should be addressed.
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)
View Full-Text   |   Download PDF [3150 KB, uploaded 22 December 2017]   |  

Abstract

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
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Magnetochemistry EISSN 2312-7481 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top