6COY
Human CLC-1 chloride ion channel, transmembrane domain
6COY の概要
| エントリーDOI | 10.2210/pdb6coy/pdb |
| 関連するPDBエントリー | 6COZ |
| EMDBエントリー | 7544 7545 |
| 分子名称 | Chloride channel protein 1, CHLORIDE ION (2 entities in total) |
| 機能のキーワード | chloride, channel, clc, transport 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 | 217608.16 |
| 構造登録者 | |
| 主引用文献 | Park, E.,MacKinnon, R. Structure of the CLC-1 chloride channel fromHomo sapiens. Elife, 7:-, 2018 Cited by PubMed Abstract: CLC channels mediate passive Cl conduction, while CLC transporters mediate active Cl transport coupled to H transport in the opposite direction. The distinction between CLC-0/1/2 channels and CLC transporters seems undetectable by amino acid sequence. To understand why they are different functionally we determined the structure of the human CLC-1 channel. Its 'glutamate gate' residue, known to mediate proton transfer in CLC transporters, adopts a location in the structure that appears to preclude it from its transport function. Furthermore, smaller side chains produce a wider pore near the intracellular surface, potentially reducing a kinetic barrier for Cl conduction. When the corresponding residues are mutated in a transporter, it is converted to a channel. Finally, Cl at key sites in the pore appear to interact with reduced affinity compared to transporters. Thus, subtle differences in glutamate gate conformation, internal pore diameter and Cl affinity distinguish CLC channels and transporters. PubMed: 29809153DOI: 10.7554/eLife.36629 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.36 Å) |
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