2IH1
Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation
2IH1 の概要
| エントリーDOI | 10.2210/pdb2ih1/pdb |
| 関連するPDBエントリー | 2IH3 |
| 分子名称 | FAB Heavy Chain, FAB Light Chain, Voltage-gated potassium channel, ... (6 entities in total) |
| 機能のキーワード | ion channel d-amino acid semi-synthetic, membrane protein |
| 由来する生物種 | Streptomyces lividans 詳細 |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: P0A334 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 60513.58 |
| 構造登録者 | Valiyaveetil, F.I.,Leonetti, M.,Muir, T.W.,MacKinnon, R. (登録日: 2006-09-25, 公開日: 2006-11-21, 最終更新日: 2024-10-09) |
| 主引用文献 | Valiyaveetil, F.I.,Leonetti, M.,Muir, T.W.,Mackinnon, R. Ion Selectivity in a Semisynthetic K+ Channel Locked in the Conductive Conformation. Science, 314:1004-1007, 2006 Cited by PubMed Abstract: Potassium channels are K+-selective protein pores in cell membrane. The selectivity filter is the functional unit that allows K+ channels to distinguish potassium (K+) and sodium (Na+) ions. The filter's structure depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+ channel containing the d-enantiomer of alanine in place of a conserved glycine and found by x-ray crystallography that its filter maintains the K+ (conductive) structure in the presence of Na+ and very low concentrations of K+. This channel conducts Na+ in the absence of K+ but not in the presence of K+. These findings demonstrate that the ability of the channel to adapt its structure differently to K+ and Na+ is a fundamental aspect of ion selectivity, as is the ability of multiple K+ ions to compete effectively with Na+ for the conductive filter. PubMed: 17095703DOI: 10.1126/science.1133415 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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