Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-1 complex.
Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-1 complex.
复制标题
骨骼肌细丝和肌球蛋白分子复合物的三维图像分析。
DOI：
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发表时间：
1985
期刊：
影响因子：
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通讯作者：
T. Wakabayashi
中科院分区：
文献类型：
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作者：
C. Toyoshima;T. Wakabayashi
为了在肌动蛋白-原肌球蛋白-肌球蛋白亚片段-1（actin-TM-S1）复合物的三维图像中分配肌动蛋白分子，将肌动蛋白-原肌球蛋白复合物的三维图像与actin-TM-S1的三维图像相关联。为了以定量的方式评估两个结构的相似性，我们使用了归一化互相关函数（“相似性函数”）。相似性计算表明，结构域A和结构域B对应于肌动蛋白原肌球蛋白。这种分配表明，一个S1分子强烈相互作用，只有一个肌动蛋白分子，但至少有两个区域的S1有助于结合。与那些装饰细丝的重构模型的比较表明，肌动蛋白分子的形状发生了变化。
To assign the actin molecule in the three-dimensional image of the actin-tropomyosin-myosin subfragment-1 (actin-TM-S1) complex, the three-dimensional image of the actin-tropomyosin complex was correlated to that of actin-TM-S1. To assess the similarity of two structures in a quantitative manner, we used a normalized cross-correlation function ("similarity function"). The calculation of similarity indicated that domain A and domain B defined in (1, 2) correspond to actin-tropomyosin. This assignment indicates that one S1 molecule strongly interacts with only one actin molecule, but at least two regions of S1 contribute to the binding. Comparison of the reconstituted models of thin filaments with those of decorated thin filaments suggested a change in the shape of the actin molecule.