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Comment
. 2013 Jul 30;110(31):12507-8.
doi: 10.1073/pnas.1310669110. Epub 2013 Jul 12.

Mutation that causes hypertrophic cardiomyopathy increases force production in human β-cardiac myosin

Affiliations
Comment

Mutation that causes hypertrophic cardiomyopathy increases force production in human β-cardiac myosin

Joseph M Muretta et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
HCM and dilated cardiomyopathy (DCM) causing β-cardiac myosin heavy chain mutations (A, magenta ribbons, R453C shown as magenta spheres) found in the myosin motor domain (4DB1 crystal structure) (3). The R453C HCM mutation is located between the HO helix (orange) and the 7-stranded β-sheet (green). Relay helix (cyan) and bound nucleotide (AMPPNP nucleotide, red spheres) shown for reference. (B) Crystal structure of β-cardiac myosin (4DB1) suggests potential hydrogen bonds between the R453 side chain and neighboring backbone oxygen atoms (Q451, and T449 shown), as well as the hydroxyl oxygen on S260 in the AMPPNP-bound state. These interactions would by altered in the R453C mutant (modeled in C), which could affect the flexibility of the β-sheet.

Comment on

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