CSL与CaV 1.2钙通道N末端的相互结合作用  

Interaction between CSL and N-terminal of CaV1.2 calcium channel

作　　者：薛迎春 张峰慧 雷帅 周诗 晏珊 严玲 邵冬雪 苏敬阳 胡慧媛 郝丽英 XUE Ying-chun;ZHANG Feng-hui;LEI Shuai;ZHOU Shi;YAN Shan;YAN Ling;SHAO Dong-xue;SUJing-yang;HU Hui-yuan;HAO Li-ying(Department of Pharmaceutical Toxicology,School of Pharmacy,China Medical University,Shenyang 110122,China)

机构地区：[1]中国医科大学药学院药物毒理学教研室,辽宁沈阳110122

出　　处：《解剖科学进展》2020年第6期622-625,629,共5页Progress of Anatomical Sciences

基　　金：国家自然科学基金青年基金(81100108);西南医科大学心血管医学研究所开放基金(201605);辽宁省教育厅科学研究项目-基础研究项目(JC2019035);大学生创新训练项目(201910159062)。

摘　　要：目的探讨钙蛋白酶抑素结构域L(CSL)与CaV1.2钙通道N末端(NT)之间的相互结合作用。方法利用I-TASSER同源建模服务器,对豚鼠CaV 1.2钙通道N末端和人源CSL蛋白进行同源建模,利用MOE软件预测CSL和NT蛋白之间的结合,并采用GST pull-down实验研究CSL和NT蛋白的结合特点。结果与MOE软件预测出CSL和NT蛋白可以结合,且在NT蛋白上存在两个结合位点;Pull-down实验进一步证实二者可以直接结合,且该结合具有CSL浓度依赖性。结论 CSL可以与NT蛋白结合,为进一步揭示CaV1.2钙通道的调节机制奠定了基础。Objective To explore the interaction between CSL and N terminus(NT) of CaV1.2 calcium channel. Methods I-TASSER homologous modeling server was used to model the N terminus of CaV1.2 calcium channel in guinea pig and CSL protein in human. MOE software was used to simulate the binding of CSL and NT protein, and then the characteristics of the binding of CSL and NT was studied by GST pull-down assay. Results It was predicted from MOE that NT could bind to the CSL protein with two binding sites on NT protein. The pull-down assay proved that NT could bind to CSL in a CSL concentration-dependent manner. Conclusion The N terminus of CaV1.2 calcium channel could bind to CSL, which laid a foundation for revealing the function and regulation mechanism of CaV1.2 calcium channel.

关 键 词：CaV1.2钙通道 钙蛋白酶抑素 MOE GST pull-down 

分 类 号：Q257[生物学—细胞生物学]