中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90

文献类型:期刊论文

作者Li, Jian(李健) ; Sun, Lihua(孙丽华) ; Xu, Chunyan(徐春艳) ; Yu, Feng(郁峰) ; Zhou, Huan ; Zhao, Yanlong ; Zhang, Jian ; Cai, Jianhua ; Mao, Cheney ; Tang, Lin(唐琳) ; Xu, Yechun ; He, Jianhua(何建华)
刊名ACTA BIOCHIMICA ET BIOPHYSICA SINICA
出版日期2012
卷号44期号:4页码:300
ISSN号1672-9145
英文摘要The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein. Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90. Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.
收录类别SCI
语种英语
WOS记录号WOS:000302297500003
公开日期2013-09-11
源URL[http://ir.sinap.ac.cn/handle/331007/12915]  
专题上海应用物理研究所_中科院上海应用物理研究所2011-2017年
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Li, Jian,Sun, Lihua,Xu, Chunyan,et al. Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2012,44(4):300.
APA Li, Jian.,Sun, Lihua.,Xu, Chunyan.,Yu, Feng.,Zhou, Huan.,...&He, Jianhua.(2012).Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,44(4),300.
MLA Li, Jian,et al."Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 44.4(2012):300.

入库方式: OAI收割

来源:上海应用物理研究所

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