朊病毒蛋白中的铜结合
Copper binding in the prion protein.
作者信息
Millhauser Glenn L
机构信息
Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, USA.
出版信息
Acc Chem Res. 2004 Feb;37(2):79-85. doi: 10.1021/ar0301678.
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.
朊病毒蛋白的构象变化引发了一类被称为传染性海绵状脑病的神经退行性疾病，其中包括疯牛病以及人类的库鲁病和克雅氏病。尽管这些疾病备受关注，但朊病毒蛋白在健康组织中的正常功能仍不清楚。然而，过去几年的研究表明，朊病毒蛋白是一种对Cu(2+)具有高选择性的铜结合蛋白。目前已经对Cu(2+)结合位点的结构特征进行了表征，这些特征为朊病毒蛋白的正常功能以及金属或蛋白质功能丧失在疾病中可能发挥的作用提供了重要线索。朊病毒蛋白与铜之间的联系可能有助于深入了解金属在神经退行性疾病中普遍且近来受到重视的作用。
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