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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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| Pubblicato in: | PLoS Comput Biol |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Public Library of Science
2017
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| Soggetti: | |
| Accesso online: | 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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