Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90 |
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Authors: | Li Jian Sun Lihua Xu Chunyan Yu Feng Zhou Huan Zhao Yanlong Zhang Jian Cai Jianhua Mao Cheney Tang Lin Xu Yechun He Jianhua |
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Affiliation: | Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China. |
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Abstract: | 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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