A) Schematic representation of PrP and the histidine residues involved in this study.

<p>The N-terminal domain contains four octapeptide repeats and one non-octarepeat site, each characterized by high affinity for copper ions (Cu 2+). The histidine residues involved in copper coordination are shown as pentagons. The globular domain contains three α-helixes and three short β-str...

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Detalles Bibliográficos
Autor Principal:	Juan-María Torres (22446393) (author)
Outros autores:	Alba Marín-Moreno (18565596) (author), Juan-Carlos Espinosa (532438) (author), Sara Canoyra (18565602) (author), Anna Burato (22446396) (author), Arianna Ciullini (21185627) (author), Chiara Maria Giulia De Luca (5124917) (author), Edoardo Bistaffa (840433) (author), Fabio Moda (332100) (author), Giuseppe Legname (26814) (author)
Publicado:	2025
Subjects:	Biochemistry Microbiology Cell Biology Genetics Molecular Biology Neuroscience Pharmacology Infectious Diseases Computational Biology neurodegenerative disorders caused mice expressing wild copper may play sc </ sup c </ sup div >< p vivo </ tga20 </ spongiform encephalopathy spongiform degeneration region located prion protein prion diseases prion disease octapeptide repeats misfolded isoform histidine 95 functional implication copper binding cellular form brain homogenate binding site 100 days
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A) Schematic representation of PrP and the histidine residues involved in this study.

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