Molecular basis of myosin assembly: coiled-coil interactions and the role of charge periodicities.

S J Atkinson, M Stewart
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引用次数: 27

Abstract

Complementation of alternating zones of positive and negative charge in the myosin rod enables molecules to interact in a number of ways. This accounts for the complexity of the molecular organisation of thick filaments. However, directed mutagenesis of expressed LMM cDNA indicated that charge zone complementation is not a major driving force in myosin polymerisation. Instead, it probably serves to prevent unfavourable interaction geometries.

肌球蛋白组装的分子基础:线圈相互作用和电荷周期性的作用。
肌凝蛋白棒中正负电荷交替带的互补使分子能够以多种方式相互作用。这就解释了粗丝分子组织的复杂性。然而,对表达的LMM cDNA的定向诱变表明,电荷区互补不是肌球蛋白聚合的主要驱动力。相反,它可能是用来防止不利的相互作用几何。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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