生物信息学Issue(2)：110-116,7.DOI:10.3969/j.issn.1672-5565.2014.02.06
Hsc70-Auxilin复合物的拉伸分子动力学模拟
Steered molecular dynamics simulations of Hsc70-Auxilin interactions
周雷 1徐利楠 2周小红 2薛友林 3李辉 2宋有涛1
作者信息
- 1. 辽宁大学环境学院，辽宁 沈阳110036
- 2. 辽宁大学生命科学院，辽宁 沈阳110036
- 3. 辽宁大学轻型产业学院，辽宁 沈阳110036
- 折叠
摘要
Abstract
The Hsc70 and auxilin complex belongs to the Hsp70 and Hsp40 family, a chaperone system best known for its role in the heat shock response. The model of the Hsc70/auxilin complex molecule used in our study had the crystal structure of disulfide-bond-crosslinked complex of bovine Hsc70 R171C and bovine auxilin D876C. In order to confirm the important residues, we first analyzed the stable model after the molecular dynamics simulation ( MD) . The binding site of the mutated ( original) model was more aligned with previous biochemical results. After that, steered molecular dynamics simulations ( SMD) were applied to this stable model to investigate the dissociation of the bovine auxilin J-domain and the Hsc70 ATPase domain, and the Hsc70-auxilin interactions were also investigated. Our data indicated that His874, Asp876, and Thr879 from the HPD loop, Glu884, Asn895, Asp896, Ser899, Glu902 and Asn903 from helix Ⅲ are important residues. These data agreed with a previous NMR evidence that helix Ⅲ and HPD motif of large T antigen J-domain interacted with Hsc70 ATPase domain.关键词
Auxilin/J-domain/Hsc70/蛋白相互作用/拉伸分子动力学Key words
Auxilin/J-domain/Hsc70/Protein-protein interactions/Steered molecular dynamics分类
生物科学引用本文复制引用
周雷,徐利楠,周小红,薛友林,李辉,宋有涛..Hsc70-Auxilin复合物的拉伸分子动力学模拟[J].生物信息学,2014,(2):110-116,7.
