Steered molecular dynamics simulations on the binding of the appendant structure and helix-beta 2 in domain-swapped human cystatin C dimer

作者：Shen Manli; Guan Jing; Xu Linan; Yu Yuanyuan; He Jianwei; Jones Gary W; Song Youtao^*

来源：Journal of Biomolecular Structure & Dynamics, 2012, 30(6): 652-661.

DOI：10.1080/07391102.2012.689698

• human cystatin C
• steered molecular dynamics
• appendant structure
• amyloid
• domain swapping

We have performed steered molecular dynamics (SMD) simulations to investigate the dissociation process between the appendant structure (AS) and helix-beta 2 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 beta 2-helix were formed following domain swapping and were responsible for stabilizing the structure of the domain-swapped dimer.

• 出版日期2012
• 单位辽宁大学