Manli Shen, Youtao Song

School of Environment

Jing Guan, Linan Xu, Yuanyuan Yu, Jianwei He

Province Key Laboratory of Animal Resource and Epidemic Disease Prevention

Gary W. Jones

National University of Ireland Maynooth

Abstract

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.

Read the article here:     118-Steered molecular dynamics simulations on the binding of the appendant structure and helix-β2 in domain-swapped human cystatin C dimer.pdf