Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 37, Issue 2, Pages 79-85Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar0301678
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Funding
- NIGMS NIH HHS [R01 GM065790-08, R01 GM065790, GM 65790] Funding Source: Medline
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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 Cu2+. The structural features of the Cu2+ 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 neuro degenerative disease.
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