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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, 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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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: 04 Jun 2017 03:45

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