Copper Binding in the Prion Protein
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Abstract
A conformational change of the prion protein is responsible for a class of neurodegenerative diseases called the transmissible spongiform encephalopathies that include mad cow disease and the human afflictions kuru and Creutzfeldt-Jakob disease. Despite the attention given to these diseases, the normal function of the prion protein in healthy tissue is unknown. Research over the past few years, however, demonstrates that the prion protein is a copper binding protein with high selectivity for Cu(2+). The structural features of the Cu(2+) binding sites have now been characterized and are providing important clues about the normal function of the prion protein and perhaps how metals or loss of protein function play a role in disease. The link between prion protein and copper may provide insight into the general, and recently appreciated, role of metals in neurodegenerative disease.
Related Papers
- → Atypical Prion Diseases in Humans and Animals(2011)46 cited
- Historical overview of prion diseases: a view from afar.(2012)
- [Prion diseases. Review of the literature on the light of two case reports of Creutzfeldt-Jakob disease].(1996)
- → Prion disease(2012)
- → Prion-protein-related diseases of animals and man(2011)