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Conformational cycling within the closed state of Grp94, an Hsp90-family chaperone
The Hsp90 family of chaperones require ATP-driven cycling to perform their function. The presence of two bound ATP molecules is known to favor a closed conformation of the Hsp90 dimer. However, the structural and mechanistic consequences of subsequent ATP hydrolysis are poorly understood. Using sing...
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| Опубликовано в: : | J Mol Biol |
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| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2019
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6697201/ https://ncbi.nlm.nih.gov/pubmed/31202885 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2019.06.004 |
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