School of Material Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.
Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Int J Mol Sci. 2021 Jun 23;22(13):6709. doi: 10.3390/ijms22136709.
The transition between strong and weak interactions of the kinesin head with the microtubule, which is regulated by the change of the nucleotide state of the head, is indispensable for the processive motion of the kinesin molecular motor on the microtubule. Here, using all-atom molecular dynamics simulations, the interactions between the kinesin head and tubulin are studied on the basis of the available high-resolution structural data. We found that the strong interaction can induce rapid large conformational changes of the tubulin, whereas the weak interaction cannot. Furthermore, we found that the large conformational changes of the tubulin have a significant effect on the interaction of the tubulin with the head in the weak-microtubule-binding ADP state. The calculated binding energy of the ADP-bound head to the tubulin with the large conformational changes is only about half that of the tubulin without the conformational changes.
头部与微管之间强相互作用和弱相互作用的转换，由头部核苷酸状态的变化来调节，这对驱动蛋白分子马达在微管上的进行性运动是必不可少的。在这里，我们使用全原子分子动力学模拟，根据现有高分辨率结构数据研究了头部与微管之间的相互作用。我们发现，强相互作用可以诱导微管的快速大构象变化，而弱相互作用则不能。此外，我们发现微管的大构象变化对弱结合 ADP 态微管中头部与微管的相互作用有显著影响。计算得到的带有大构象变化的 ADP 结合头部与微管的结合能约为没有构象变化的微管的一半。
