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微管相关蛋白tau的结构与弹性

Structure and elasticity of microtubule-associated protein tau.

作者信息

Lichtenberg B, Mandelkow E M, Hagestedt T, Mandelkow E

机构信息

Max-Planck-Unit for Structural Molecular Biology, Hamburg, FRG.

出版信息

Nature. 1988 Jul 28;334(6180):359-62. doi: 10.1038/334359a0.

Abstract

Tau is one of the diverse group of microtubule-associated proteins that bind to microtubules and may thereby influence their structure and function. It occurs in the mammalian brain, mainly in axons, and is a component of the neurofibrillary tangles of Alzheimer's disease. Tau was recently sequenced, but there remains a short-age of structural data on the protein. We have now prepared paracrystals of tau suitable for electron microscopy and image processing. They show distinct transverse banding and polarity, indicating that the protein subunits are aligned with the same orientations. In contrast to other paracrystals, those of tau protein can stretch or contract continuously by more than three-fold; the axial repeats range from 22 to 68 nm. After scaling to a common period, the density distributions are closely superimposable. This suggests that tau is an elastic molecule.

摘要

tau蛋白是多种微管相关蛋白之一,它与微管结合,从而可能影响微管的结构和功能。它存在于哺乳动物大脑中,主要在轴突中,是阿尔茨海默病神经原纤维缠结的一个组成部分。tau蛋白最近已被测序,但关于该蛋白质的结构数据仍然短缺。我们现已制备出适合电子显微镜观察和图像处理的tau蛋白准晶体。它们呈现出明显的横向条纹和极性,表明蛋白质亚基以相同方向排列。与其他准晶体不同,tau蛋白的准晶体可以连续拉伸或收缩三倍以上;轴向重复距离在22至68纳米之间。在按共同周期缩放后,密度分布紧密重叠。这表明tau蛋白是一种弹性分子。

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