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肌球蛋白II的结构研究:远距离蛋白质结构域之间的通讯

Structural studies on myosin II: communication between distant protein domains.

作者信息

Gulick A M, Rayment I

机构信息

Institute for Enzyme Research, University of Wisconsin, Madison 53705, USA.

出版信息

Bioessays. 1997 Jul;19(7):561-9. doi: 10.1002/bies.950190707.

DOI:10.1002/bies.950190707
PMID:9230689
Abstract

Understanding how chemical energy is converted into directed movement is a fundamental problem in biology. In higher organisms this is accomplished through the hydrolysis of ATP by three families of motor proteins: myosin, dynein and kinesin. The most abundant of these is myosin, which operates against actin and plays a central role in muscle contraction. As summarized here, great progress has been made towards understanding the molecular basis of movement through the determination of the three-dimensional structures of myosin and actin and through the establishment of systems for site-directed mutagenesis of this motor protein. It now appears that the generation of movement is coupled to ATP hydrolysis by a series of domain movements within myosin.

摘要

了解化学能如何转化为定向运动是生物学中的一个基本问题。在高等生物中,这是通过三类驱动蛋白水解ATP来实现的:肌球蛋白、动力蛋白和驱动蛋白。其中最丰富的是肌球蛋白,它作用于肌动蛋白,在肌肉收缩中起核心作用。如下所述,通过确定肌球蛋白和肌动蛋白的三维结构以及建立该驱动蛋白的定点诱变系统,在理解运动的分子基础方面已经取得了很大进展。现在看来,运动的产生与肌球蛋白内一系列结构域的运动与ATP水解相关联。

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