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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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| Publicat a: | PLoS Comput Biol |
|---|---|
| Autors principals: | , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Public Library of Science
2017
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5608440/ https://ncbi.nlm.nih.gov/pubmed/28892477 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pcbi.1005748 |
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