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Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions
Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides. To understand the mechanism by which the Hsp104 N-terminal domain (NTD) interacts with its peptide substrates, crystal structures of the Hsp104 NTDs from Saccharomyces cerev...
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| Gepubliceerd in: | Acta Crystallogr D Struct Biol |
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| Hoofdauteurs: | , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
International Union of Crystallography
2017
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6688567/ https://ncbi.nlm.nih.gov/pubmed/28375147 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2059798317002662 |
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