Structural Consequences of Copper Binding to the Prion Protein

Prion, or PrP(Sc), is the pathological isoform of the cellular prion protein (PrP(C)) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrP(C) is its ability to bind copper ions through its flexible N...

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Autores principales: Salzano, Giulia, Giachin, Gabriele, Legname, Giuseppe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721516/
https://www.ncbi.nlm.nih.gov/pubmed/31349611
http://dx.doi.org/10.3390/cells8080770
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author Salzano, Giulia
Giachin, Gabriele
Legname, Giuseppe
author_facet Salzano, Giulia
Giachin, Gabriele
Legname, Giuseppe
author_sort Salzano, Giulia
collection PubMed
description Prion, or PrP(Sc), is the pathological isoform of the cellular prion protein (PrP(C)) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrP(C) is its ability to bind copper ions through its flexible N-terminal moiety. This review includes an overview of the structure and function of PrP(C) with a focus on its ability to bind copper ions. The state-of-the-art of the role of copper in both PrP(C) physiology and in prion pathogenesis is also discussed. Finally, we describe the structural consequences of copper binding to the PrP(C) structure.
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spelling pubmed-67215162019-09-10 Structural Consequences of Copper Binding to the Prion Protein Salzano, Giulia Giachin, Gabriele Legname, Giuseppe Cells Review Prion, or PrP(Sc), is the pathological isoform of the cellular prion protein (PrP(C)) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrP(C) is its ability to bind copper ions through its flexible N-terminal moiety. This review includes an overview of the structure and function of PrP(C) with a focus on its ability to bind copper ions. The state-of-the-art of the role of copper in both PrP(C) physiology and in prion pathogenesis is also discussed. Finally, we describe the structural consequences of copper binding to the PrP(C) structure. MDPI 2019-07-25 /pmc/articles/PMC6721516/ /pubmed/31349611 http://dx.doi.org/10.3390/cells8080770 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Salzano, Giulia
Giachin, Gabriele
Legname, Giuseppe
Structural Consequences of Copper Binding to the Prion Protein
title Structural Consequences of Copper Binding to the Prion Protein
title_full Structural Consequences of Copper Binding to the Prion Protein
title_fullStr Structural Consequences of Copper Binding to the Prion Protein
title_full_unstemmed Structural Consequences of Copper Binding to the Prion Protein
title_short Structural Consequences of Copper Binding to the Prion Protein
title_sort structural consequences of copper binding to the prion protein
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721516/
https://www.ncbi.nlm.nih.gov/pubmed/31349611
http://dx.doi.org/10.3390/cells8080770
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