Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations

Cytoplasmic dynein is a giant ATP-driven molecular motor that proceeds to the minus end of the microtubule (MT). Dynein hydrolyzes ATP in a ring-like structure, containing 6 AAA+ (ATPases associated with diverse cellular activities) modules, which is ~15 nm away from the MT binding domain (MTBD). Th...

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Detalles Bibliográficos
Autores principales: Kubo, Shintaroh, Li, Wenfei, Takada, Shoji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5608440/
https://www.ncbi.nlm.nih.gov/pubmed/28892477
http://dx.doi.org/10.1371/journal.pcbi.1005748

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5608440/
https://www.ncbi.nlm.nih.gov/pubmed/28892477
http://dx.doi.org/10.1371/journal.pcbi.1005748

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