STRUCTURE DETERMINATION OF RPRP GENE PRODUCT: PRIONS

朊病毒是仅由蛋白质组成的感染剂。 它们引起 人类和动物的许多疾病。 模式 感染涉及蛋白质结构的变化， β折叠形式。 我们已经完善了阿尔法的解决方案结构 叙利亚仓鼠PrP基因重组片段螺旋形式 产品 已知这种朊病毒蛋白存在于至少两种 不同的构象。 一种溶液形式主要是 α螺旋（PrPc）和另一种聚集的β折叠形式（PrP 瘙痒症）。 结构二态性本身是有趣的，因为它 表明氨基酸序列可以编码多个 结构，但更重要的是，序列在 人类病理学，因为它涉及朊病毒疾病。 这 该项目对药物设计都具有重要意义，而且，在更大程度上， 基础水平，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，我们开始检查 另一种具有类似特性的蛋白质，tau蛋白。 这种蛋白质 也经历了构象变化， 老年痴呆症

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.