Mornet D, Bertrand R, Pantel P, Audemard E, Kassab R
Nature. 1981 Jul 23;292(5821):301-6. doi: 10.1038/292301a0.
The topography of the rigor complex between F-actin and myosin heads (S1) has been investigated by carbodiimide zero-length cross-linking. The results demonstrate for the first time that the 95,000-molecular weight (95K) heavy chain of the myosin head enters into van der Waals contact with two neighbouring actin monomers; one is bound to the 50K domain and the other to the 20K domain of the myosin chain. The covalent F-actin-S1 complex can be isolated; it shows a vastly elevated Mg2+-ATPase. Each pair of actin subunits in the thin filament seems to act as a functional unit for specific binding of a myosin head and stimulation of its Mg2+-ATPase activity.
通过碳二亚胺零长度交联法研究了F-肌动蛋白与肌球蛋白头部（S1）之间僵直复合体的拓扑结构。结果首次表明，肌球蛋白头部95,000分子量（95K）的重链与两个相邻的肌动蛋白单体形成范德华接触；一个与肌球蛋白链的50K结构域结合，另一个与20K结构域结合。可以分离出共价的F-肌动蛋白-S1复合体；它显示出大大提高的Mg2 + -ATP酶活性。细肌丝中的每对肌动蛋白亚基似乎都作为一个功能单元，用于肌球蛋白头部的特异性结合并刺激其Mg2 + -ATP酶活性。
