Structural Consequences of Copper Binding to the Prion Protein
Prion, or PrP<sup>Sc</sup>, is the pathological isoform of the cellular prion protein (PrP<sup>C</sup>) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrP<sup>C</su...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2019-07-01
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| Series: | Cells |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4409/8/8/770 |
| Summary: | Prion, or PrP<sup>Sc</sup>, is the pathological isoform of the cellular prion protein (PrP<sup>C</sup>) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrP<sup>C</sup> 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<sup>C</sup> with a focus on its ability to bind copper ions. The state-of-the-art of the role of copper in both PrP<sup>C</sup> physiology and in prion pathogenesis is also discussed. Finally, we describe the structural consequences of copper binding to the PrP<sup>C</sup> structure. |
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| ISSN: | 2073-4409 |