Assessment of the Contribution of a Thermodynamic and Mechanical Destabilization of Myosin-Binding Protein C Domain C2 to the Pathomechanism of Hypertrophic Cardiomyopathy-Causing Double Mutation <i>MYBPC3</i><sup>Δ<i>25bp/D389V</i></sup>

Assessment of the Contribution of a Thermodynamic and Mechanical Destabilization of Myosin-Binding Protein C Domain C2 to the Pathomechanism of Hypertrophic Cardiomyopathy-Causing Double Mutation <i>MYBPC3</i><sup>Δ<i>25bp/D389V</i></sup>

Mutations in the gene encoding cardiac myosin-binding protein-C (MyBPC), a thick filament assembly protein that stabilizes sarcomeric structure and regulates cardiac function, are a common cause for the development of hypertrophic cardiomyopathy. About 10% of carriers of the Δ25bp variant of <i&g...

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Bibliographic Details
Main Authors: Frederic V. Schwäbe, Emanuel K. Peter, Manuel H. Taft, Dietmar J. Manstein
Format: Article
Language:English
Published: MDPI AG 2021-11-01
Series:International Journal of Molecular Sciences
Subjects:
hypertrophic cardiomyopathy
heart disorder
MyBPC
enhanced molecular dynamics simulations
allosteric trigger
cardiac contractility
Online Access:https://www.mdpi.com/1422-0067/22/21/11949

Internet

https://www.mdpi.com/1422-0067/22/21/11949

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