2V6H

Crystal structure of the C1 domain of cardiac myosin binding protein-C

Summary for 2V6H

• Entry DOI: 10.2210/pdb2v6h/pdb
• Related: 1GXE 1PD6
• Descriptor: MYOSIN-BINDING PROTEIN C, CARDIAC-TYPE (2 entities in total)
• Functional Keywords: cell adhesion, phosphorylation, mybp-c c1 domain, disease mutation, muscle regulation, igi domain structure, muscle protein, cardiomyopathy, thick filament, immunoglobulin domain, hypertropic cardiomyopathy, polymorphism, actin-binding
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 12049.61

Authors

Govata, L.,Carpenter, L.,Da Fonseca, P.C.A.,Helliwell, J.R.,Rizkallah, P.J.,Flashman, E.,Chayen, N.E.,Redwood, C.,Squire, J.M. (deposition date: 2007-07-18, release date: 2008-07-22, Last modification date: 2024-05-08)

Primary citation

Govada, L.,Carpenter, L.,da Fonseca, P.C.,Helliwell, J.R.,Rizkallah, P.,Flashman, E.,Chayen, N.E.,Redwood, C.,Squire, J.M.
Crystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathy.
J. Mol. Biol., 378:387-397, 2008

PubMed 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 A. 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.

PubMed: 18374358
DOI: 10.1016/j.jmb.2008.02.044

Experimental method

X-RAY DIFFRACTION (1.55 Å)