Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
A. N. Bakh Institute of Biochemistry, Federal Research Center Fundamentals of Biotechnology, Russian Academy of Sciences, Moscow, Russia.
Bull Exp Biol Med. 2024 Jan;176(3):324-327. doi: 10.1007/s10517-024-06017-y. Epub 2024 Feb 10.
Cardiac myosin binding protein-C (cMyBP-C) located in the C-zone of myocyte sarcomere is involved in the regulation of myocardial contraction. Its N-terminal domains C0, C1, C2, and the m-motif between C1 and C2 can bind to the myosin head and actin of the thin filament and affect the characteristics of their interaction. Measurements using an optical trap showed that the C0-C2 fragment of cMyBP-C increases the interaction time of cardiac myosin with the actin filament, while in an in vitro motility assay, it dose-dependently reduces the sliding velocity of actin filaments. Thus, it was found that the N-terminal part of cMyBP-C affects the kinetics of the myosin cross-bridge.
心肌球蛋白结合蛋白 C（cMyBP-C）位于肌节的 C 带区，参与心肌收缩的调节。其 N 端结构域 C0、C1、C2 和 C1 与 C2 之间的 m 基序可与肌球蛋白头部和细肌丝上的肌动蛋白结合，并影响它们相互作用的特征。光学捕获测量表明，cMyBP-C 的 C0-C2 片段增加了肌球蛋白与肌动蛋白丝的相互作用时间，而在体外运动分析中，它呈浓度依赖性地降低了肌动蛋白丝的滑行速度。因此，人们发现 cMyBP-C 的 N 端部分影响肌球蛋白横桥的动力学。
