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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural changes of membrane-anchored native PrP~C
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Structural changes of membrane-anchored native PrP~C

机译：膜锚定天然PrP〜C的结构变化

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摘要

Misfolding and subsequent aggregation of endogeneous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully posttranslationally modified cellular prion protein, carrying two N-glycosylations and the natural GPI anchor. We used time-resolved FTIR to study the prion protein secondary structure changes when binding to a raft-like lipid membrane via its GPI anchor. We observed that membrane anchoring above a threshold concentration induced refolding of the prion protein to intermolecular β-sheets. Such transition is not observed in solution and is membrane specific. Excessive membrane anchoring, analyzed with molecular sensitivity, is thought to be a crucial event in the development of prion diseases.
机译：内源性蛋白质的错误折叠和随后的聚集是许多人类疾病（包括阿尔茨海默病和病毒疾病）中必不可少的步骤。在大多数病毒蛋白质折叠研究中，缺少翻译后修饰，尤其是脂质锚。在这里，我们研究了经过完全翻译后修饰的细胞病毒蛋白，带有两个N-糖基化和天然GPI锚。我们使用时间分辨FTIR研究了via蛋白通过其GPI锚点与筏状脂质膜结合时二级结构的变化。我们观察到高于阈值浓度的膜锚定诱导病毒蛋白重折叠至分子间β-折叠。这种过渡在溶液中未观察到，并且是膜特异性的。用分子敏感性分析过多的膜锚定被认为是of病毒疾病发展中的关键事件。

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