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Copper coordination modulates prion conversion and infectivity in mammalian prion proteins

In mammals the cellular form of the prion protein (PrP(C)) is a ubiquitous protein involved in many relevant functions in the central nervous system. In addition to its physiological functions PrP(C) plays a central role in a group of invariably fatal neurodegenerative disorders collectively called...

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Detalles Bibliográficos
Autor principal: Legname, Giuseppe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9815218/
https://www.ncbi.nlm.nih.gov/pubmed/36597284
http://dx.doi.org/10.1080/19336896.2022.2163835
Descripción
Sumario:In mammals the cellular form of the prion protein (PrP(C)) is a ubiquitous protein involved in many relevant functions in the central nervous system. In addition to its physiological functions PrP(C) plays a central role in a group of invariably fatal neurodegenerative disorders collectively called prion diseases. In fact, the protein is a substrate in a process in which it converts into an infectious and pathological form denoted as prion. The protein has a unique primary structure where the unstructured N-terminal moiety possesses characteristic sequences wherein histidines are able to coordinate metal ions, in particular copper ions. These sequences are called octarepeats for their characteristic length. Moreover, a non-octarepeat fifth-copper binding site is present where copper coordination seems to control infectivity. In this review, I will argue that these sequences may play a significant role in modulating prion conversion and replication.