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The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis
Hsp90, a dimeric ATP-dependent molecular chaperone, is required for the folding and activation of numerous essential substrate “client” proteins including nuclear receptors, cell cycle kinases, and telomerase. Fundamental to its mechanism is an ensemble of dramatically different conformational state...
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| Hoofdauteurs: | , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Wiley Subscription Services, Inc., A Wiley Company
2012
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3537237/ https://ncbi.nlm.nih.gov/pubmed/22653663 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2103 |
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