doi:10.12202/j.0476-0301.2020199尹燕霞^1,,
佟丽¹,
黄建华²,
姜国华^{1, 2,,}
1.北京师范大学生命科学学院，北京市基因工程药物及生物技术重点实验室，100875，北京
2.北京师范大学分析测试中心，100875，北京
基金项目:国家自然科学基金资助项目（30770478）

详细信息

通讯作者:姜国华（1962—），男，博士，教授. 研究方向：蛋白质结构和功能. E-mail：jgh982@bnu.edu.cn

中图分类号:Q556

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出版历程

收稿日期:2020-05-18
网络出版日期:2021-01-21
刊出日期:2021-05-08

Structure and function of calcineurin B subunit: mutation in the calcium binding site

Yanxia YIN^1,,
Li TONG¹,
Jianhua HUANG²,
Guohua JIANG^{1, 2,,}
1. College of Life Sciences, Beijing Key Laboratory of Genetic Engineering Drugs and Biotechnology, Beijing Normal University, 100875, Beijing, China
2. Analysis and Testing Center, Beijing Normal University, 100875, Beijing, China



摘要
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摘要
摘要:应用远紫外CD光谱、紫外差光谱、内源荧光光谱以及ANS荧光光谱，探究了钙调磷酸酶B亚基钙结合位点的突变对B亚基结构和功能的影响．结果显示：钙结合位点突变体Y105W激活CNA的能力强于CNB；而E110Q活化CNA的能力弱于CNB；Y105W和E110Q与Ca²⁺亲和性低于CNB；CNB和它的突变体二级结构趋于一致，但三级结构存在明显差异，这种差异可能是它们功能差异的结构基础．
关键词:钙调磷酸酶/
Ca²⁺/
磷酸酶活性/
三级结构/
钙结合位点
Abstract:Effect of mutations in the calcium binding site on calcineurin B subunit structure and function was investigated, by far ultraviolet CD spectrum, ultraviolet difference spectrum, endogenous fluorescence spectrum and ANS fluorescence spectrum．It was found that calcium binding site mutant CNB-Y105W was stronger than wild type CNB to activate CNA, but CNB-E110Q was weaker．The affinity of CNB-Y105W and CNB-E110Q for Ca²⁺ was both found to be lower than CNB．The secondary structures were found to be similar among CNB and the 2 mutants, but their tertiary structures showed significant differences, consistent with their differences in protein activity．
Key words:calcineurin/
Ca²⁺/
phosphatase activity/
tertiary structure/
calcium binding site