Periodicities designed in the tropomyosin sequence and structure define its functions.
Periodicities designed in the tropomyosin sequence and structure define its functions.
复制标题
DOI：
10.4161/bioa.25616
复制
发表时间：
2013-05-01
期刊：
影响因子：
--
通讯作者：
Barua, Bipasha
中科院分区：
文献类型：
--
作者：
Barua, Bipasha
原肌球蛋白是一种肌动蛋白结合蛋白，在大多数真核细胞中调节肌动蛋白细丝的动力学及其与肌球蛋白、原肌球蛋白、Forin、Arp2/3和ADF-cofilin等肌动蛋白结合蛋白的相互作用。原肌球蛋白是一种典型的双链、α螺旋螺旋卷曲蛋白，它与肌动蛋白细丝的两端相连并结合在一起。根据原肌球蛋白的大小，每个原肌球蛋白分子跨越细丝中的四到七个肌动蛋白单体。原肌球蛋白有一个周期性的七肽重复序列，这是卷曲蛋白的特征，以及它与肌动蛋白细丝相互作用所需的额外周期，其中每个周期性重复与一个肌动蛋白分子相互作用。本文综述了TM分子的周期性特征在执行其与肌动蛋白细丝结合的普遍功能中的作用及其调节，以及可能决定原肌球蛋白异构体特异性的具体特征。
Tropomyosin is an actin binding protein that regulates actin filament dynamics and its interactions with actin binding proteins such as myosin, tropomodulin, formin, Arp2/3 and ADF-cofilin in most eukaryotic cells. Tropomyosin is the prototypical two-chained, alpha-helical coiled coil protein that associates end-to-end and binds to both sides of the actin filament. Each tropomyosin molecule spans four to seven actin monomers in the filament, depending on the size of the tropomyosin. Tropomyosins have a periodic heptad repeat sequence that is characteristic of coiled coil proteins as well as additional periodicities required for its interaction with the actin filament, where each periodic repeat interacts with one actin molecule. This review addresses the role of periodic features of the Tm molecule in carrying out its universal functions of binding to the actin filament and its regulation and the specific features that may determine the isoform specificity of tropomyosins.