A flipped ion pair at the dynein–microtubule interface is critical for dynein motility and ATPase activation

Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis...

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Detalles Bibliográficos
Autores principales: Uchimura, Seiichi, Fujii, Takashi, Takazaki, Hiroko, Ayukawa, Rie, Nishikawa, Yosuke, Minoura, Itsushi, Hachikubo, You, Kurisu, Genji, Sutoh, Kazuo, Kon, Takahide, Namba, Keiichi, Muto, Etsuko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2015
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4298687/
https://www.ncbi.nlm.nih.gov/pubmed/25583999
http://dx.doi.org/10.1083/jcb.201407039

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4298687/
https://www.ncbi.nlm.nih.gov/pubmed/25583999
http://dx.doi.org/10.1083/jcb.201407039

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