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微管蛋白与影响微管动力学的蛋白质和药物相互作用的结构基础。

Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics.

作者信息

Downing K H

机构信息

Donner Laboratory, Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

出版信息

Annu Rev Cell Dev Biol. 2000;16:89-111. doi: 10.1146/annurev.cellbio.16.1.89.

Abstract

The microtubule cytoskeleton is a highly regulated system. At different times in the cell cycle and positions within the organism, microtubules can be very stable or highly dynamic. Stability and dynamics are regulated by interaction with a large number of proteins that themselves may change at specific points in the cell cycle. Exogenous ligands can disrupt the normal processes by either increasing or decreasing microtubule stability and inhibiting their dynamic behavior. The recent determination of the structure of tubulin, the main component of microtubules, makes it possible now to begin to understand the details of these interactions. We review here the structure of the tubulin dimer, with particular regard to how proteins and drugs may bind and modulate microtubule dynamics.

摘要

微管细胞骨架是一个受到高度调控的系统。在细胞周期的不同时间以及生物体内的不同位置,微管可以非常稳定,也可以高度动态变化。稳定性和动态性通过与大量蛋白质的相互作用来调节,而这些蛋白质本身在细胞周期的特定时间点可能会发生变化。外源性配体可以通过增加或降低微管稳定性以及抑制其动态行为来扰乱正常过程。最近对微管主要成分微管蛋白结构的测定,使得现在有可能开始了解这些相互作用的细节。我们在此回顾微管蛋白二聚体的结构,特别关注蛋白质和药物如何结合并调节微管动力学。

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