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可变表面环与肌球蛋白活性:运动蛋白的辅助因素

Variable surface loops and myosin activity: accessories to a motor.

作者信息

Murphy C T, Spudich J A

机构信息

Department of Biochemistry, Stanford University School of Medicine, CA 94305, USA.

出版信息

J Muscle Res Cell Motil. 2000 Feb;21(2):139-51. doi: 10.1023/a:1005610007209.

Abstract

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.

摘要

肌球蛋白的催化头部是一种球状结构,历史上它被分为25 kDa、50 kDa和20 kDa的三个片段。连接这三个片段的肌球蛋白溶剂暴露且对蛋白酶敏感的表面环在序列上高度可变。虽然传统上认为表面环不影响酶活性,但这些环位于ATP和肌动蛋白结合位点附近,并与肌球蛋白动力学活性的调节有关。在这项工作中,我们回顾了多年来积累的关于这些环的大量数据,并讨论了这些环在不同肌球蛋白同工型所表现出的不同活性中所起的作用。

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