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首页> 外文期刊>Journal of Molecular Biology >NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171.
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NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171.

机译：20℃时库田vol病毒蛋白的NMR结构包含残基165-171的结构环。

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摘要

The recent introduction of bank vole (Clethrionomys glareolus) as an additional laboratory animal for research on prion diseases revealed an important difference when compared to the mouse and the Syrian hamster, since bank voles show a high susceptibility to infection by brain homogenates from a wide range of diseased species such as sheep, goats, and humans. In this context, we determined the NMR structure of the C-terminal globular domain of the recombinant bank vole prion protein (bvPrP) [bvPrP(121-231)] at 20 degrees C. bvPrP(121-231) has the same overall architecture as other mammalian PrPs, with three alpha-helices and an antiparallel beta-sheet, but it differs from PrP of the mouse and most other mammalian species in that the loop connecting the second beta-strand and helix alpha2 is precisely defined at 20 degrees C. This is similar to the previously described structures of elk PrP and the designed mouse PrP (mPrP) variant mPrP[S170N,N174T](121-231), whereas Syrian hamster PrP displays a structure that is in-between these limiting cases. Studies with the newly designed variant mPrP[S170N](121-231), which contains the same loop sequence as bvPrP, now also showed that the single-amino-acid substitution S170N in mPrP is sufficient for obtaining a well-defined loop, thus providing the rationale for this local structural feature in bvPrP.
机译：最近引进的银行田鼠（Clethrionomys glareolus）作为研究病毒疾病的另一种实验动物，与小鼠和叙利亚仓鼠相比，发现了重要的区别，因为银行田鼠对广泛范围内的脑匀浆的感染表现出很高的敏感性。诸如绵羊，山羊和人类等患病物种。在这种情况下，我们确定了在20摄氏度时重组银行田e病毒蛋白（bvPrP）[bvPrP（121-231）]的C端球形结构的NMR结构。bvPrP（121-231）具有相同的总体结构与其他哺乳动物的PrP一样，具有三个alpha螺旋和一个反平行的β-折叠，但它与小鼠和大多数其他哺乳动物的PrP不同，在于连接第二个β链和螺旋alpha2的环精确地定义在20摄氏度这类似于先前描述的麋鹿PrP和设计的小鼠PrP（mPrP）变体mPrP [S170N，N174T]（121-231）的结构，而叙利亚仓鼠PrP显示的结构介于这些限制情况之间。使用新设计的变体mPrP [S170N]（121-231）进行的研究（其环序列与bvPrP相同）现在还显示，mPrP中的单氨基酸取代S170N足以获得定义明确的环，因此提供了bvPrP中此局部结构特征的基本原理。

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