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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon- mediated inhibition of actin filament velocity
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Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon- mediated inhibition of actin filament velocity

机译：肌钙蛋白介导的肌动蛋白丝速度的抑制作用需要平滑肌caldesmon上的N端肌球蛋白结合位点和C端肌动蛋白结合位点

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摘要

It has been suggested that the tethering caused by binding of the N-terminal region of smooth muscle caldesmon (CaD) to myosin and its C-terminal region to actin contributes to the inhibition of actin-filament movement over myosin heads in an in vitro motility assay. However, direct evidence for this assumption has been lacking. In this study, analysis of baculo- virus-generated N-terminal and C-terminal deletion mutants of chicken-gizzard CaD revealed that the major myosin-binding site on the CaD molecule resides in a 30-amino acid stretch between residues 24 and 53, based on the very low level of binding of CaD△24-53 lacking the residues 24-53 to myosin compared with the level of binding of CaD△54-85 missing the adjacent residues 54-85 or of the full-length CaD.
机译：有人提出，在体外运动中，平滑肌Caldesmon（CaD）的N端区域与肌球蛋白结合，而其C端区域与肌动蛋白结合引起的束缚作用，有助于抑制肌动蛋白丝在肌球蛋白头上的运动分析。但是，缺乏这种假设的直接证据。在这项研究中，对杆状病毒产生的鸡g CaD的N端和C端缺失突变体的分析表明，CaD分子上的主要肌球蛋白结合位点位于残基24和53之间的30个氨基酸的片段中。 ，基于缺少残基24-53与肌球蛋白的CaD△24-53的结合水平与缺失相邻残基54-85或全长CaD的CaD△54-85的结合水平相比非常低。

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