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Structural Biochemistry of Muscle Contraction.
Wang, Zhexin; Raunser, Stefan.
Afiliación
  • Wang Z; Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany; email: stefan.raunser@mpi-dortmund.mpg.de.
  • Raunser S; Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany; email: stefan.raunser@mpi-dortmund.mpg.de.
Annu Rev Biochem ; 92: 411-433, 2023 06 20.
Article en En | MEDLINE | ID: mdl-37001141
ABSTRACT
Muscles are essential for movement and heart function. Contraction and relaxation of muscles rely on the sliding of two types of filaments-the thin filament and the thick myosin filament. The thin filament is composed mainly of filamentous actin (F-actin), tropomyosin, and troponin. Additionally, several other proteins are involved in the contraction mechanism, and their malfunction can lead to diverse muscle diseases, such as cardiomyopathies. We review recent high-resolution structural data that explain the mechanism of action of muscle proteins at an unprecedented level of molecular detail. We focus on the molecular structures of the components of the thin and thick filaments and highlight the mechanisms underlying force generation through actin-myosin interactions, as well as Ca2+-dependent regulation via the dihydropyridine receptor, the ryanodine receptor, and troponin. We particularly emphasize the impact of cryo-electron microscopy and cryo-electron tomography in leading muscle research into a new era.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Actinas / Contracción Muscular Idioma: En Revista: Annu Rev Biochem Año: 2023 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Actinas / Contracción Muscular Idioma: En Revista: Annu Rev Biochem Año: 2023 Tipo del documento: Article