Variable surface loops and myosin activity: Accessories to a motor

被引：36

作者：

Murphy, CT

Spudich, JA ^{[1
]}

机构：

[1] Stanford Univ, Med Ctr, Sch Med, Dept Biochem, Stanford, CA 94305 USA

[2] Stanford Univ, Sch Med, Dept Dev Biol, Stanford, CA 94305 USA

来源：

JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY | 2000年 / 21卷 / 02期

关键词：

D O I：

10.1023/A:1005610007209

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The catalytic head of myosin is a globular structure that has historically been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed, proteolytically-sensitive surface loops of myosin that join these three segments are highly variable in their sequences. While surface loops have not traditionally been thought to affect enzymatic activities, these loops lie near the ATP and actin-binding sites and have been implicated in the modulation of myosin's kinetic activities. In this work we review the wealth of data regarding the loops that has accumulated over the years and discuss the roles of the loops in contributing to the different activities displayed by different myosin isoforms.

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页码：139 / 151

页数：13

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