The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41 | |
Cheng JiaGao2; Zhu WeiLiang1,3; Wang Yanli2; Yan XiuHua1; Li Zhong2; Tang Yun2; Jiang HuaLiang1,2 | |
刊名 | SCIENCE IN CHINA SERIES B-CHEMISTRY |
2008-08 | |
卷号 | 51期号:8页码:768-775 |
关键词 | cation-pi interaction hydrogen bond noncovalent interaction ab initio calculation M2 protein |
ISSN号 | 1006-9291 |
DOI | 10.1007/s11426-008-0087-3 |
文献子类 | Article |
英文摘要 | The M2 protein from influenza A virus is a tetrameric ion channel. It was reported that the permeation of the ion channel is correlated with the hydrogen bond network among His37 residues and the cation-pi interactions between His37 and Trp41. In the present study, the hydrogen bonding network of 4-methyl-imidazoles was built to mimic the hydrogen bonds between His37 residues, and the cation-pi interactions between 4-methyl-imidazolium and indole systems were selected to represent the interactions between His37 and Trp41. Then, quantum chemistry calculations at the MP2/6-311G** level were carried out to explore the properties of the hydrogen bonds and the cation-pi interactions. The calculation results indicate that the binding strength of the N--H center dot center dot center dot N hydrogen bond between imidazole rings is up to -6.22 kcal.mol(-1), and the binding strength of the strongest cation-pi interaction is up to -18.8 kcal.mol(-1) (T-shaped interaction) or -12.3 kcal.mol(-1) (parallel stacking interaction). Thus, the calculated binding energies indicate that it is possible to control the permeation of the M2 ion channel through the hydrogen bond network and the cation-pi interactions by altering the pH values. |
WOS关键词 | M(2) ION-CHANNEL ; PROTON CHANNEL ; ACTIVATION ; HISTIDINE ; SIMULATION ; COMPLEXES ; BILAYER |
WOS研究方向 | Chemistry |
语种 | 英语 |
出版者 | SCIENCE PRESS |
WOS记录号 | WOS:000257751300009 |
内容类型 | 期刊论文 |
源URL | [http://119.78.100.183/handle/2S10ELR8/272860] |
专题 | 药物发现与设计中心 |
通讯作者 | Zhu WeiLiang |
作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr, Shanghai 201203, Peoples R China; 2.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China; 3.E China Univ Sci & Technol, Sch Sci, Shanghai 200237, Peoples R China |
推荐引用方式 GB/T 7714 | Cheng JiaGao,Zhu WeiLiang,Wang Yanli,et al. The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41[J]. SCIENCE IN CHINA SERIES B-CHEMISTRY,2008,51(8):768-775. |
APA | Cheng JiaGao.,Zhu WeiLiang.,Wang Yanli.,Yan XiuHua.,Li Zhong.,...&Jiang HuaLiang.(2008).The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41.SCIENCE IN CHINA SERIES B-CHEMISTRY,51(8),768-775. |
MLA | Cheng JiaGao,et al."The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41".SCIENCE IN CHINA SERIES B-CHEMISTRY 51.8(2008):768-775. |
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