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Crystal structure of the C1 domain of cardiac myosin binding protein-C: Implications for hypertrophic cardiomyopathy

Govada, Lata, Carpenter, Liz, da Fonseca, Paula C. A., Helliwell, John R., Rizkallah, Pierre ORCID: https://orcid.org/0000-0002-9290-0369, Flashman, Emily, Chayen, Naomi E., Redwood, Charles and Squire, John M. 2008. Crystal structure of the C1 domain of cardiac myosin binding protein-C: Implications for hypertrophic cardiomyopathy. Journal of Molecular Biology 378 (2) , pp. 387-397. 10.1016/j.jmb.2008.02.044

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Abstract

C-protein is a major component of skeletal and cardiac muscle thick filaments. Mutations in the gene encoding cardiac C-protein [cardiac myosin binding protein-C (cMyBP-C)] are one of the principal causes of hypertrophic cardiomyopathy. cMyBP-C is a string of globular domains including eight immunoglobulin-like and three fibronectin-like domains termed C0–C10. It binds to myosin and titin, and probably to actin, and may have both a structural and a regulatory role in muscle function. To help to understand the pathology of the known mutations, we have solved the structure of the immunoglobulin-like C1 domain of MyBP-C by X-ray crystallography to a resolution of 1.55 Å. Mutations associated with hypertrophic cardiomyopathy are clustered at one end towards the C-terminus, close to the important C1C2 linker, where they alter the structural integrity of this region and its interactions.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
R Medicine > R Medicine (General)
Uncontrolled Keywords: hypertrophic cardiomyopathy, IgI domain structure, muscle regulation, MyBP-C C1 domain, c-protein
Publisher: Elsevier
ISSN: 0022-2836
Last Modified: 20 Oct 2022 07:40
URI: https://orca.cardiff.ac.uk/id/eprint/26019

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