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Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
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)
2012
Source PublicationACTA BIOCHIMICA ET BIOPHYSICA SINICA
ISSN1672-9145
Volume44Issue:4Pages:300
AbstractThe 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.
Indexed BySCI
Language英语
Funding Project应物所项目组
WOS IDWOS:000302297500003
Citation statistics
Cited Times:38[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/12915
Collection中科院上海应用物理研究所2011-2019年
Recommended Citation
GB/T 7714
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.
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