捕捉机制中的匹配分子。
Matching molecules in the catch mechanism.
作者信息
Cohen C
出版信息
Proc Natl Acad Sci U S A. 1982 May;79(10):3176-8. doi: 10.1073/pnas.79.10.3176.
Abstract
A new structural model is advanced to account for the specialized "catch" contraction of molluscan smooth muscles. The myosin of the thick filaments of these muscles is pictured as comprising a single layer of molecules whose assembly and activity are controlled by the underlying core of paramyosin. This organization differs from that in other muscles in which the myosin is grouped into bundles. The catch state--in which the lifetime of the actin-myosin linkage is extended--would depend directly on this special organization that allows an interaction of the entire rod region of myosin with the paramyosin core. This interaction might be modulated by phosphorylation of paramyosin.
摘要
提出了一种新的结构模型来解释软体动物平滑肌特有的“牵张”收缩。这些肌肉粗肌丝中的肌球蛋白被描绘为由单层分子组成，其组装和活性由原肌球蛋白的基础核心控制。这种组织形式与其他肌肉不同，在其他肌肉中肌球蛋白聚集成束。“牵张”状态（其中肌动蛋白 - 肌球蛋白连接的寿命延长）将直接取决于这种特殊组织，该组织允许肌球蛋白的整个杆状区域与原肌球蛋白核心相互作用。这种相互作用可能通过原肌球蛋白的磷酸化来调节。
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