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-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.