7CH1
The overall structure of SLC26A9
7CH1 の概要
| エントリーDOI | 10.2210/pdb7ch1/pdb |
| EMDBエントリー | 30368 |
| 分子名称 | Solute carrier family 26 member 9, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
| 機能のキーワード | membrane protein |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 174321.68 |
| 構造登録者 | Chi, X.M.,Chen, Y.,Li, X.R.,Zhang, Y.Y.,Zhou, Q. (登録日: 2020-07-03, 公開日: 2020-08-26, 最終更新日: 2024-03-27) |
| 主引用文献 | Chi, X.,Jin, X.,Chen, Y.,Lu, X.,Tu, X.,Li, X.,Zhang, Y.,Lei, J.,Huang, J.,Huang, Z.,Zhou, Q.,Pan, X. Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence. Cell Discov, 6:55-55, 2020 Cited by PubMed Abstract: The human SLC26 transporter family exhibits various transport characteristics, and family member SLC26A9 performs multiple roles, including acting as Cl/HCO exchangers, Cl channels, and Na transporters. Some mutations of SLC26A9 are correlated with abnormalities in respiration and digestion systems. As a potential target colocalizing with CFTR in cystic fibrosis patients, SLC26A9 is of great value in drug development. Here, we present a cryo-EM structure of the human SLC26A9 dimer at 2.6 Å resolution. A segment at the C-terminal end is bound to the entry of the intracellular vestibule of the putative transport pathway, which has been proven by electrophysiological experiments to be a gating modulator. Multiple chloride and sodium ions are resolved in the high-resolution structure, identifying novel ion-binding pockets for the first time. Together, our structure takes important steps in elucidating the structural features and regulatory mechanism of SLC26A9, with potential significance in the treatment of cystic fibrosis. PubMed: 32818062DOI: 10.1038/s41421-020-00193-7 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.6 Å) |
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