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• W1760677314 abstract "The conversion of the prion protein (PrP(C)) into prions plays a key role in transmissible spongiform encephalopathies. Despite the importance for pathogenesis, the mechanism of prion formation has escaped detailed characterization due to the insoluble nature of prions. PrP(C) interacts with copper through octarepeat and non-octarepeat binding sites. Copper coordination to the non-octarepeat region has garnered interest due to the possibility that this interaction may impact prion conversion. We used X-ray absorption spectroscopy to study copper coordination at pH 5.5 and 7.0 in human PrP(C) constructs, either wild-type (WT) or carrying pathological mutations. We show that mutations and pH cause modifications of copper coordination in the non-octarepeat region. In the WT at pH 5.5, copper is anchored to His96 and His111, while at pH 7 it is coordinated by His111. Pathological point mutations alter the copper coordination at acidic conditions where the metal is anchored to His111. By using in vitro approaches, cell-based and computational techniques, we propose a model whereby PrP(C) coordinating copper with one His in the non-octarepeat region converts to prions at acidic condition. Thus, the non-octarepeat region may act as the long-sought-after prion switch, critical for disease onset and propagation." @default.
• W1760677314 created "2016-06-24" @default.
• W1760677314 creator A5002905256 @default.
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• W1760677314 date "2015-10-20" @default.
• W1760677314 modified "2023-10-12" @default.
• W1760677314 title "The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion" @default.
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• W1760677314 doi "https://doi.org/10.1038/srep15253" @default.
• W1760677314 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4651146" @default.
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• W1760677314 hasPublicationYear "2015" @default.
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