Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Biochemistry (Mosc). 2011 Dec;76(13):1507-27. doi: 10.1134/S0006297911130098.
This review concerns the structure and functions of tropomyosin (TM), an actin-binding protein that plays a key role in the regulation of muscle contraction. The TM molecule is a dimer of α-helices, which form a coiled-coil. Recent views on the TM structure are analyzed, and special attention is concentrated on those structural traits of the TM molecule that distinguish it from the other coiled-coil proteins. Modern data are presented on TM functional properties, such as its interaction with actin and ability to move on the surface of actin filaments, which underlies the regulation of the actin-myosin interaction upon contraction of skeletal and cardiac muscles. Also, part of the review is devoted to analysis of the effects of mutations in TM genes associated with muscle diseases (myopathies) on the structure and functions of TM.
这篇综述涉及原肌球蛋白（TM）的结构和功能，TM 是一种肌动蛋白结合蛋白，在肌肉收缩的调节中起着关键作用。TM 分子是由α-螺旋组成的二聚体，形成了一个卷曲螺旋。分析了 TM 结构的最新观点，并特别关注了将 TM 分子与其他卷曲螺旋蛋白区分开来的结构特征。介绍了 TM 功能特性的现代数据，例如它与肌动蛋白的相互作用以及在肌动蛋白丝表面移动的能力，这是调节骨骼肌和心肌收缩时肌球蛋白与肌动蛋白相互作用的基础。此外，综述的一部分还致力于分析与肌肉疾病（肌病）相关的 TM 基因突变对 TM 结构和功能的影响。
