Province Key Laboratory of Animal Resource and Epidemic Disease Prevention, Liaoning University, Shenyang, 110036, China.
J Biomol Struct Dyn. 2012;30(6):652-61. doi: 10.1080/07391102.2012.689698. Epub 2012 Jun 26.
We have performed steered molecular dynamics (SMD) simulations to investigate the dissociation process between the appendant structure (AS) and helix-β2 in human cystatin C dimer. Energy change during SMD showed that electrostatic interactions, including hydrogen bonds and salt bridges, were the dominant interactions to stabilize the two parts of the dimer. Furthermore, our data indicated that residues, Asn35, Asp40, Ser44, Lys75, and Arg93 play significant roles in the formation of these electrostatic interactions. Docking studies suggested that the interactions between AS and β2-helix were formed following domain swapping and were responsible for stabilizing the structure of the domain-swapped dimer.
我们进行了导向分子动力学（SMD）模拟，以研究人半胱氨酸蛋白酶抑制剂 C 二聚体中附属结构（AS）与β2-螺旋之间的解离过程。SMD 过程中的能量变化表明，静电相互作用，包括氢键和盐桥，是稳定二聚体两部分的主要相互作用。此外，我们的数据表明，残基 Asn35、Asp40、Ser44、Lys75 和 Arg93 在这些静电相互作用的形成中发挥了重要作用。对接研究表明，AS 与β2-螺旋之间的相互作用是通过结构域交换形成的，负责稳定结构域交换二聚体的结构。
