Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein
Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein
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DOI：
10.1016/j.jmb.2008.03.035
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发表时间：
2008-05-16
影响因子：
5.6
通讯作者：
Chan, Jerry C. C.
中科院分区：
文献类型：
--
作者：
Lee, Shin-Wen;Mou, Yun;Chan, Jerry C. C.
我们报告的结果，原子力显微镜，傅里叶变换红外光谱，固态核磁共振，和分子动力学（MD）计算的淀粉样蛋白原纤维形成的残基109122的叙利亚仓鼠朊病毒蛋白（H1）。我们的数据显示，H1原纤维包含不超过两个β-折叠层。H1原纤维的肽链与A117残基反向平行排列，在原纤维轴的方向上形成直链。H1纤维的分子结构，它采用了空间拉链的基序，是高度均匀的回文序列AGAAAAGA的区域。发现两个相邻β-片层之间的最近距离为约5埃。分子动力学模拟得到的H1纤维分子模型的结构特征与实验结果一致。总的来说，我们的固态NMR和MD模拟数据表明，空间拉链，这是第一次观察到的晶体中的原纤维形成肽，可以形成在H1原纤维附近的回文序列的区域。(C)2008爱思唯尔有限公司版权所有。
We report the results of atomic force microscopy, Fourier-transform infrared spectroscopy, solid-state nuclear magnetic resonance, and molecular dynamics (MD) calculations for amyloid fibrils formed by residues 109122 of the Syrian hamster prion protein (H1). Our data reveal that H1 fibrils contain no more than two beta-sheet layers. The peptide strands of H1 fibrils are antiparallel with the A117 residues aligned to form a linear chain in the direction of the fibril axis. The molecular structure of the H1 fibrils, which adopts the motif of steric zipper, is highly uniform in the region of the palindrome sequence AGAAAAGA. The closest distance between the two adjacent beta-sheet layers is found to be about 5 angstrom. The structural features of the molecular model of H1 fibrils obtained by MD simulations are consistent with the experimental results. Overall, our solid-state NMR and MD simulation data indicate that a steric zipper, which was first observed in the crystals of fibril-forming peptides, can be formed in H1 fibrils near the region of the palindrome sequence. (C) 2008 Elsevier Ltd. All rights reserved.