Related Experiment Video
Updated: Jan 21, 2026

Detection of Abnormal Prion Protein by Immunohistochemistry
Published on: May 5, 2023
Structural Consequences of Copper Binding to the Prion Protein
Giulia Salzano1, Gabriele Giachin2, Giuseppe Legname3,4
1Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy.
Abstract:
Prion, or PrPSc, is the pathological isoform of the cellular prion protein (PrPC) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrPC is its ability to bind copper ions through its flexible N-terminal moiety. This review includes an overview of the structure and function of PrPC with a focus on its ability to bind copper ions. The state-of-the-art of the role of copper in both PrPC physiology and in prion pathogenesis is also discussed. Finally, we describe the structural consequences of copper binding to the PrPC structure.
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Structural Protein Function
Protein and Protein Structures
Timing and Consequences on Behavior
Humans, however, can respond to delayed reinforcers. We often make decisions between immediate small rewards and delayed larger rewards. This ability to delay gratification is a significant...
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...

