详细信息
Interaction of calcineurin with its activator, chlorogenic acid revealed by spectroscopic methods ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Interaction of calcineurin with its activator, chlorogenic acid revealed by spectroscopic methods
作者:Yin, Yanxia[1];Xie, Mengxia[1];Wu, Hezhen[1];Jiang, Min[1];Zheng, Jianquan[2];Wei, Qun[1]
第一作者:Yin, Yanxia
通讯作者:Wei, Q[1]
机构:[1]Beijing Normal Univ, Dept Biochem & Mol Biol, Beijing Key Lab, Beijing 100875, Peoples R China;[2]Beijing Union Univ, Beijing Lab Bioact Subst & Funct Foods, Beijing 100083, Peoples R China
第一机构:Beijing Normal Univ, Dept Biochem & Mol Biol, Beijing Key Lab, Beijing 100875, Peoples R China
通讯机构:[1]corresponding author), Beijing Normal Univ, Dept Biochem & Mol Biol, Beijing Key Lab, Beijing 100875, Peoples R China.
年份:2009
卷号:91
期号:7
起止页码:820-825
外文期刊名:BIOCHIMIE
收录:;Scopus(收录号:2-s2.0-67349170802);WOS:【SCI-EXPANDED(收录号:WOS:000267628700002)】;
基金:This work was supported in part by a grant from the National Natural Science Foundation of China, the Research Fund for the Doctoral Program of Higher Education and the National important Basal Research Project and the Association Project of the Ministry of Education and GuangDong Province.
语种:英文
外文关键词:Calcineurin; Chlorogenic acid; Activators; Interaction
摘要:Chlorogenic acid (CHA) has been proved to be an activator of calcineurin (CN) in our previous research. In this study, the activation of single chain calcineurin (BA) by CHA, their interaction and concomitant changes in protein conformation were studied using fluorescence and Fourier transform infrared spectroscopy. Evidence is present that binding of CHA to CN is responsible for the stimulation of enzyme and results in structural changes. Aromatic residues reorient into new environments upon binding of CHA, the binding constant for the reaction was (2.76 +/- 0.64) x 10(4) M-1 by one binding site, which indicated that CHA bound to BA statically and the change of secondary structure was mainly due to reduced a-helical content and increased beta-turns. The results obtained in this study should be useful for understanding the molecular mechanisms underlying the interactions between CN and its activators. (C) 2009 Elsevier Masson SAS. All rights reserved.
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