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The Affinity of the Dynein Microtubule-Binding Domain is Modulated by the Conformation of its Coiled-Coil Stalk

The microtubule binding domain (MTBD) of dynein is separated from the AAA core of the motor by an ~15 nm stalk that is predicted to consist of an anti-parallel coiled coil. However, the structure of this coiled-coil and the mechanism it uses to mediate communication between the MTBD and ATP-binding...

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Detaylı Bibliyografya
Asıl Yazarlar: Gibbons, I. R., Garbarino, Joan E., Tan, Carol E., Reck-Peterson, Samara L., Vale, Ronald D., Carter, Andrew P.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 2005
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1464088/
https://ncbi.nlm.nih.gov/pubmed/15826937
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M501636200
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