STRUCTURE DETERMINATION OF RPRP GENE PRODUCT: PRIONS

普恩病毒是一种仅由蛋白质组成的感染剂。它们会导致 人类和动物身上都有一些疾病。一种新模式 感染涉及蛋白质结构的变化，从α螺旋到 测试版表单。我们已经改进了阿尔法的解决方案结构 叙利亚仓鼠PrP基因重组片段的螺旋形式 产品。这种蛋白已知存在于至少两种 不同的构象。一种主要的解决方案形式 阿尔法螺旋(PrPc)和另一种聚集的β-片状(PrP 瘙痒病)。结构二态本身就很有趣，因为它 演示了氨基酸序列可以编码多个 结构，但更重要的是，该序列在 人类的病理，因为它与普恩病毒疾病有关。这 该项目对药物设计和更多 基本层面，我们理解蛋白质折叠的能力。现在 我们已经完成了这个结构，我们正在开始检查 另一种具有类似性质的蛋白质是tau蛋白。这种蛋白质 也经历了构象变化，这涉及到 阿尔茨海默氏症。

Prions are infections agents made up of protein only. They cause a number of diseases in both humans and animals. The mode of infection involves a protein structural change from alpha helical to beta sheet form. We have refined the solution structure of the alpha helical form of a recombinant fragment of syrian hamster PrP gene product. This prion protein is known to exist in at least two different conformations. One solution form that is predominantly alpha helical (PrPc) and another, aggregated beta-sheet form (PrP Scrapie). The structural dimorphism in itself is interesting since it demonstrates that amino acid sequences can encode more than one structure, but more importantly, the sequence has significance in human pathology because it is involved in prion diseases. This project is significant for both drug design, and, on a more fundamental level, our ability to understand protein folding. Now that we have completed this structure we are beginning to examine another protein with similar properties, protein tau. This protein also undergoes a conformational change that is involved with Alzheimer's disease.