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微管蛋白的晶体结构:对动力学和药物结合的影响。

Crystallographic structure of tubulin: implications for dynamics and drug binding.

作者信息

Downing K H, Nogales E

机构信息

Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

出版信息

Cell Struct Funct. 1999 Oct;24(5):269-75. doi: 10.1247/csf.24.269.

Abstract

The structure of tubulin, recently solved by electron crystallography, has given a first look at the molecular basis for some of the properties of tubulin and microtubules that have been observed over the last decades. We discuss how the structure relates to some of these properties, and how inferences about drug binding sites can explain some of the effects of the drugs on tubulin. Microtubules can form a highly dynamic system that requires careful tuning of the stability and properties of tubulin and its interactions with its many ligands. Understanding these interactions can provide fundamental information on the regulation of the microtubule system.

摘要

微管蛋白的结构最近通过电子晶体学得以解析,这让我们首次了解到过去几十年来所观察到的微管蛋白和微管某些特性的分子基础。我们将探讨该结构与其中一些特性的关联,以及关于药物结合位点的推断如何解释这些药物对微管蛋白的某些作用。微管可形成一个高度动态的系统,这需要对微管蛋白的稳定性、特性及其与众多配体的相互作用进行精细调节。了解这些相互作用能够为微管系统的调控提供基础信息。

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