Mechanism of unusual AQP6 activation by mercury binding to a pore-external residue C155
文献类型：期刊论文
| 作者 | Ma, Shaojie1,2,3; Xie, Huayong3; Yu, Kunqian4 ; Yang, Jun1,2,3
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| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2022-08-27 |
| 卷号 | 618页码:1-7 |
| 关键词 | Aquaporins Activation mechanism MD simulations Pore-external residue |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2022.06.025 |
| 文献子类 | Article |
| 英文摘要 | Aquaporins (AQPs) transport water molecules across cell membranes. Although most aquaporins are inhibited by mercury ions, AQP6 was reported to be activated by binding mercury ions to residues C155 and C190. Different from C190 and the other pore-line cysteine residues, C155 is located outside the pore, thus not directly affecting the internal pathway by mercury binding to it. The molecular mechanism of unusual water channel activation by mercury ion binding to the C155 site remains unknown. Here, we investigate the activation of AQP6 by mercury ions binding to C155 by molecular dynamics (MD) simulations. The MD simulation results show that the mercury-induced water permeation activation is derived from the conformational change of a pore-line residue M160, from a point-to-pore conformation before mercury binding to an away-pore conformation after mercury binding. The conformation change of M160 is derived from the reduction of the hydrogen bonding between C155 and S159 in the alpha-helix with the coordination of C155 to mercury ion altering their conformation significantly. This study reveals the complex mechanism of water channel activation by mercury ion binding to pore-external residues in water channels. (C) 2022 Elsevier Inc. All rights reserved. |
| WOS关键词 | WATER PERMEABILITY ; AQUAPORIN ; PERMEATION ; INHIBITION |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000827684400001 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/309337]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Yu, Kunqian; Yang, Jun |
| 作者单位 | 1.Huazhong Univ Sci & Technol, Collaborat Innovat Ctr Brain Sci, Key Lab Mol Biophys Minist Educ, Wuhan 430074, Peoples R China; 2.Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Key Lab Mol Biophys Minist Educ, Wuhan 430074, Peoples R China; 3.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan Inst Phys & Math, Natl Ctr Magnet Resonance Wuhan,Key Lab Magnet Res, Wuhan 430071, Peoples R China; 4.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr, State Key Lab Drug Res, Shanghai 201203, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ma, Shaojie,Xie, Huayong,Yu, Kunqian,et al. Mechanism of unusual AQP6 activation by mercury binding to a pore-external residue C155[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2022,618:1-7. |
| APA | Ma, Shaojie,Xie, Huayong,Yu, Kunqian,&Yang, Jun.(2022).Mechanism of unusual AQP6 activation by mercury binding to a pore-external residue C155.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,618,1-7. |
| MLA | Ma, Shaojie,et al."Mechanism of unusual AQP6 activation by mercury binding to a pore-external residue C155".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 618(2022):1-7. |
入库方式： OAI收割
来源：上海药物研究所
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