Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.

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Detalles Bibliográficos
Autores principales: Doris Hellerschmied, Anita Lehner, Nina Franicevic, Renato Arnese, Chloe Johnson, Antonia Vogel, Anton Meinhart, Robert Kurzbauer, Luiza Deszcz, Linn Gazda, Michael Geeves, Tim Clausen
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Science
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Acceso en línea:https://doaj.org/article/988d6ef9a9a34ef79788fa29755892f7
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Sumario:Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.

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