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Half-Site Inhibition of Dimeric Kinesin Head Domains by Monomeric Tail Domains
The two heavy chains of kinesin-1 are dimerized through extensive coiled coil regions and fold into an inactive conformation through interaction of the C-terminal tail domains with the N-terminal motor (head) domains. Although this potentially allows a dimer of tail domains to interact symmetrically...
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| Главные авторы: | , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2009
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3321547/ https://ncbi.nlm.nih.gov/pubmed/19320433 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi8022575 |
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