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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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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2005
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| Témata: | |
| On-line přístup: | 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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