8AMX
AQP7 dimer of tetramers_D4
8AMX の概要
エントリーDOI | 10.2210/pdb8amx/pdb |
EMDBエントリー | 15528 |
分子名称 | Aquaporin-7 (2 entities in total) |
機能のキーワード | membrane channel, octamer, adhesion protein, junction protein, membrane protein |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 298115.16 |
構造登録者 | Huang, P.,Venskutonyte, R.,Fan, X.,Li, P.,Yan, N.,Gourdon, P.,Lindkvist-Petersson, K. (登録日: 2022-08-04, 公開日: 2023-02-15, 最終更新日: 2024-07-24) |
主引用文献 | Huang, P.,Venskutonyte, R.,Prasad, R.B.,Ardalani, H.,de Mare, S.W.,Fan, X.,Li, P.,Spegel, P.,Yan, N.,Gourdon, P.,Artner, I.,Lindkvist-Petersson, K. Cryo-EM structure supports a role of AQP7 as a junction protein. Nat Commun, 14:600-600, 2023 Cited by PubMed Abstract: Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas. PubMed: 36737436DOI: 10.1038/s41467-023-36272-y 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.55 Å) |
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