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A Low Affinity Ground State Conformation for the Dynein Microtubule Binding Domain
Dynein interacts with microtubules through a dedicated binding domain that is dynamically controlled to achieve high or low affinity, depending on the state of nucleotide bound in a distant catalytic pocket. The active sites for microtubule binding and ATP hydrolysis communicate via conformational c...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2010
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2871468/ https://ncbi.nlm.nih.gov/pubmed/20351100 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.083535 |
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