换一批Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
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.
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DOI
10.1093/abbs/gms001
发布时间
2012-07-27（万方平台首次上网日期，不代表论文的发表时间）
基金项目
the National Program on Key Basic Research Project（(2011CB911102)）
Shanghai Institute of Applied Physics, Chinese Academy of Sciences（(O95501C061)）
the Important National Science & Technology Specific Projects（(2010ZX09401-401)）
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