Kajiyama H
Department of Physics, Faculty of Science, University of Tokyo, Japan.
J Mol Biol. 1988 Dec 5;204(3):639-52. doi: 10.1016/0022-2836(88)90361-0.
The structure of the actin-tropomyosin-heavy meromyosin rigor complex was studied by image analysis of electron micrographs. The arrowhead of the rigor complex has a whisker-like structure with a dense turning point at the "barb" of the arrowhead. The neck region of the myosin head in the reconstructed three-dimensional image is present in the area corresponding to the dense point. It is concluded that at least one extra-thin area contributes to the neck region, and that the two heads in the heavy meromyosin molecule join a double helical rope beyond the end of the large head (G in this study). (This is different from previous interpretations). It is also concluded that the heavy meromyosin has a short bent part near the head/rod junction in the rigor complex.
通过电子显微镜照片的图像分析研究了肌动蛋白-原肌球蛋白-重酶解肌球蛋白僵直复合体的结构。僵直复合体的箭头状结构具有类似须的结构,在箭头的“倒刺”处有一个致密的转折点。重建三维图像中肌球蛋白头部的颈部区域位于对应致密点的区域。得出的结论是,至少有一个超薄区域构成颈部区域,并且重酶解肌球蛋白分子中的两个头部在大头(本研究中的G)末端之外连接成一条双螺旋绳索。(这与之前的解释不同)。还得出结论,在僵直复合体中,重酶解肌球蛋白在头部/杆连接处附近有一个短的弯曲部分。