调控差异肌球蛋白 II 类的常见结构基序。
Common structural motifs for the regulation of divergent class II myosins.
机构信息
Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont 05405, USA.
出版信息
J Biol Chem. 2010 May 28;285(22):16403-7. doi: 10.1074/jbc.R109.025551. Epub 2010 Mar 25.
Abstract
This minireview focuses on structural studies that have provided insights into our current understanding of thick filament regulation in muscle. We describe how different domains in the myosin molecule interact to produce an inactive "off" state; included are head-head and head-rod interactions, the role of the regulatory light chain, and the significance of the alpha-helical coiled-coil rod in regulation. Several of these interactions have now been visualized in a wide variety of native myosin filaments, testifying to the generality of these structural motifs across the phylogenetic tree.
摘要
本篇综述聚焦于结构研究，这些研究为我们目前对肌肉中粗肌丝调节的理解提供了深入的见解。我们描述了肌球蛋白分子中的不同结构域如何相互作用产生无活性的“关闭”状态，包括头部-头部和头部-杆之间的相互作用、调节轻链的作用以及α-螺旋卷曲杆在调节中的重要性。这些相互作用中的几个现在已经在各种天然肌球蛋白纤维中得到了可视化，证明了这些结构基序在整个系统发育树上的普遍性。
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