globalchange  > 气候变化与战略
DOI: 10.1016/j.scib.2020.12.006
论文题名:
The structural basis for glycerol permeation by human AQP7
作者: Zhang L.; Yao D.; Xia Y.; Zhou F.; Zhang Q.; Wang Q.; Qin A.; Zhao J.; Li D.; Li Y.; Zhou L.; Cao Y.
刊名: Science Bulletin
ISSN: 20959273
出版年: 2021
卷: 66, 期:15
起始页码: 1550
结束页码: 1558
语种: 英语
中文关键词: Aquaglyceroporins ; Glycerol metabolism ; Glycerol transportation ; Structural biology
英文关键词: Cell proliferation ; Molecular dynamics ; Aromatic residues ; Glycerol channels ; Molecular dynamics simulations ; Pancreatic islet ; Physiological condition ; Selectivity filter ; Structural basis ; Substrate binding ; Glycerol
英文摘要: Human glycerol channel aquaporin 7 (AQP7) conducts glycerol release from adipocyte and enters the cells in pancreatic islets, muscles, and kidney tubules, and thus regulates glycerol metabolism in those tissues. Compared with other human aquaglyceroporins, AQP7 shows a less conserved “NPA” motif in the center cavity and a pair of aromatic residues at Ar/R selectivity filter. To understand the structural basis for the glycerol conductance, we crystallized the human AQP7 and determined the structure at 3.7 Å. A substrate binding pocket was found near the Ar/R filter where a glycerol molecule is bound and stabilized by R229. Glycerol uptake assay on human AQP7 as well as AQP3 and AQP10 demonstrated strong glycerol transportation activities at the physiological condition. The human AQP7 structure, in combination with the molecular dynamics simulation thereon, reveals a fully closed conformation with its permeation pathway strictly confined by the Ar/R filter at the exoplasmic side and the gate at the cytoplasmic side, and the binding of glycerol at the Ar/R filter plays a critical role in controlling the glycerol flux by driving the dislocation of the residues at narrowest parts of glycerol pathway in AQP7. © 2021 Science China Press
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/170503
Appears in Collections:气候变化与战略

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作者单位: CAS Center for Excellence on Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, 201210, China; Institute of Precision Medicine, The Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200125, China; iHuman Institute, ShanghaiTech University, Shanghai, 201210, China; Department of Orthopaedics, Shanghai Key Laboratory of Orthopaedic Implant, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China; Department of Medicinal Chemistry, School of Pharmacy, Fudan University, Shanghai, 200433, China

Recommended Citation:
Zhang L.,Yao D.,Xia Y.,et al. The structural basis for glycerol permeation by human AQP7[J]. Science Bulletin,2021-01-01,66(15)
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