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Intra- and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90
Nucleotide-dependent conformational changes of the constitutively dimeric molecular chaperone Hsp90 are integral to its molecular mechanism. Recent full-length crystal structures (Protein Data Bank codes 2IOQ, 2CG9, AND 2IOP) of Hsp90 homologs reveal large scale quaternary domain rearrangements upon...
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| Главные авторы: | , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2008
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2475720/ https://ncbi.nlm.nih.gov/pubmed/18492664 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M800046200 |
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