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从微管蛋白的原子模型看微管结构与功能的新见解。

New insights into microtubule structure and function from the atomic model of tubulin.

作者信息

Downing K H, Nogales E

机构信息

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

出版信息

Eur Biophys J. 1998;27(5):431-6. doi: 10.1007/s002490050153.

Abstract

The structure of tubulin has recently been solved by electron crystallography of zinc-induced tubulin sheets. Because tubulin was studied in a polymerized state, the model contains information on the interactions between monomers that give rise to the alpha beta dimer as well as contacts between adjacent dimers that result in the structure of the protofilament. The model includes the binding site of taxol, an anti-cancer agent that acts by stabilizing microtubules. The present tubulin model gives the first structural framework for understanding microtubule polymerization and its regulation by nucleotides and anti-mitotic drugs at the molecular level.

摘要

微管蛋白的结构最近通过锌诱导的微管蛋白片层的电子晶体学得以解析。由于微管蛋白是在聚合状态下进行研究的,该模型包含了有关形成αβ二聚体的单体间相互作用以及导致原纤维结构的相邻二聚体间接触的信息。该模型包括紫杉醇的结合位点,紫杉醇是一种通过稳定微管起作用的抗癌药物。目前的微管蛋白模型为在分子水平上理解微管聚合及其受核苷酸和抗有丝分裂药物的调控提供了首个结构框架。

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