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Article

The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.

Scientific reports - 20 Oct 2015

Giachin Gabriele, Mai Phuong Thao, Tran Thanh Hoa, Salzano Giulia, Benetti Federico, Migliorati Valentina, Arcovito Alessandro, Della Longa Stefano, Mancini Giordano, D'Angelo Paola, Legname Giuseppe

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26482532
DOI: 10.1038/srep15253
PMCID: PMC4651146

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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