Steered molecular dynamics simulations on the binding of the appendant structure and helix-β2 in domain-swapped human cystatin C dimer

被引：20

作者：

Shen, Manli ^{[1
,2
]}

Guan, Jing ^{[1
]}

Xu, Linan ^{[1
]}

Yu, Yuanyuan ^{[1
]}

He, Jianwei ^{[1
]}

Jones, Gary W. ^{[3
]}

Song, Youtao ^{[1
,2
]}

机构：

[1] Liaoning Univ, Prov Key Lab Anim Resource & Epidem Dis Prevent, Shenyang 110036, Peoples R China

[2] Liaoning Univ, Sch Environm Sci, Shenyang 110036, Peoples R China

[3] Natl Univ Ireland Maynooth, Dept Biol, Maynooth, Kildare, Ireland

来源：

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2012年 / 30卷 / 06期

基金：

中国国家自然科学基金;

关键词：

human cystatin C; steered molecular dynamics; appendant structure; amyloid; domain swapping; PROTEIN OLIGOMERIZATION; CRYSTAL-STRUCTURE; REVEALS; DOCKING;

D O I：

10.1080/07391102.2012.689698

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：652 / 661

页数：10

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