2MQ0: NMR structure of the c3 domain of human cardiac myosin binding protein-c

Human cardiac myosin binding protein C (cMyBP-C), a thick filament protein found within the sarcomere of cardiac muscle, regulates muscle contraction and is essential for proper muscle function. Hypertrophic cardiomyopathy (HCM), a genetic disease affecting 1 in 500 people, is the major cause of death in young athletes. It is caused by genetic mutations within sarcomeric proteins. Forty-two percent of the HCM-related mutations are found in cMyBP-C. Here we present the nuclear magnetic resonance-derived structural ensembles of the wild-type cMyBP-C C3 domain and its HCM-related R502W mutant. The C3 domain adopts an immunoglobulin-like fold, and mutation of the exposed Arg502 to a tryptophan does not perturb its structure, dynamics, or stability. However, the R502W mutation does alter the predicted electrostatic properties of the C3 domain. We hypothesize that this mutation, and other HCM-linked mutations found within the same domain, may directly disrupt the interaction of cMyBP-C with other sarcomeric proteins.
PDB ID: 2MQ0Download
MMDB ID: 121835
PDB Deposition Date: 2014/6/10
Updated in MMDB: 2014/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MQ0: monomeric; determined by author
Molecular Components in 2MQ0
Label Count Molecule
Protein (1 molecule)
Myosin-binding Protein C, Cardiac-type(Gene symbol: MYBPC3)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB