北京大学医学部机构知识库
Advanced  
IR@PKUHSC  > 基础医学院  > 北京大学系统生物医学研究所  > 期刊论文
学科主题: 基础医学
题名:
Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function
作者: Liu, Liang1,2,3; Chen, Ji-Yun1,2; Yang, Bo3; Wang, Fang-Hua4; Wang, Yong-Hua4; Yun, Cai-Hong1,2
刊名: STRUCTURE
发表日期: 2015-11-03
DOI: 10.1016/j.str.2015.08.015
卷: 23, 期:11, 页:2066-2075
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
研究领域[WOS]: Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]: ALPHA-B-CRYSTALLIN ; SUBSTRATE-BINDING ; UNFOLDED PROTEIN ; T4 LYSOZYME ; DOMAIN ; SOFTWARE ; HSP16.5 ; STRESS ; HSP26 ; OLIGOMERIZATION
英文摘要:

Small heat-shock proteins (sHsps) maintain cellular homeostasis by binding to denatured client proteins to prevent aggregation. Numerous studies indicate that the N-terminal domain (NTD) of sHsps is responsible for binding to client proteins, but the binding mechanism and chaperone activity regulation remain elusive. Here, we report the crystal structures of the wild-type and mutants of an sHsp from Sulfolobus solfataricus representing the inactive and active state of this protein, respectively. All three structures reveal well-defined NTD, but their conformations are remarkably different. The mutant NTDs show disrupted helices presenting a reformed hydrophobic surface compatible with recognizing client proteins. Our functional data show that mutating key hydrophobic residues in this region drastically altered the chaperone activity of this sHsp. These data suggest a new model in which a molecular switch located in NTD facilitates conformational changes for client protein binding.

语种: 英语
所属项目编号: 2012CB917202 ; 31270769 ; NCET-12-0013 ; 31222043 ; 2014ZM0062
项目资助者: National Basic Research Program of China (973 Program) ; National Science Foundation of China ; Ministry of Science and Technology of China ; National Science Funds for the Excellent Youth Scholars ; fundamental Research Funds for the Central Universities
WOS记录号: WOS:000366170300013
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/54662
Appears in Collections:基础医学院_北京大学系统生物医学研究所_期刊论文

Files in This Item:
File Name/ File Size Content Type Version Access License
1-s2.0-S0969212615003652-main.pdf(2646KB)期刊论文作者接受稿限制开放 联系获取全文

作者单位: 1.Peking Univ, Beijing Key Lab Tumor Syst Biol, Hlth Sci Ctr, Inst Syst Biomed,Dept Biophys,Sch Basic Med Sci, Beijing 100191, Peoples R China
2.Peking Univ, Hlth Sci Ctr, Sch Basic Med Sci, Ctr Mol & Translat Med, Beijing 100191, Peoples R China
3.S China Univ Technol, Sch Biosci & Bioengn, Guangzhou 510006, Guangdong, Peoples R China
4.S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510641, Guangdong, Peoples R China

Recommended Citation:
Liu, Liang,Chen, Ji-Yun,Yang, Bo,et al. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function[J]. STRUCTURE,2015,23(11):2066-2075.
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Liu, Liang]'s Articles
[Chen, Ji-Yun]'s Articles
[Yang, Bo]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Liu, Liang]‘s Articles
[Chen, Ji-Yun]‘s Articles
[Yang, Bo]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
Add to CiteULike Add to Connotea Add to Del.icio.us Add to Digg Add to Reddit
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Copyright © 2007-2017  北京大学医学部 - Feedback
Powered by CSpace