Toyoshima C, Wakabayashi T
J Biochem. 1985 Jan;97(1):245-63. doi: 10.1093/oxfordjournals.jbchem.a135049.
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.
为了在肌动蛋白-原肌球蛋白-肌球蛋白亚片段1(肌动蛋白-TM-S1)复合物的三维图像中确定肌动蛋白分子,将肌动蛋白-原肌球蛋白复合物的三维图像与肌动蛋白-TM-S1的三维图像进行了关联。为了以定量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,(1, 2)中定义的结构域A和结构域B对应于肌动蛋白-原肌球蛋白。这一确定表明,一个S1分子仅与一个肌动蛋白分子强烈相互作用,但S1的至少两个区域参与结合。将重构的细肌丝模型与标记的细肌丝模型进行比较,提示肌动蛋白分子的形状发生了变化。