2QTS

Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH

2QTS の概要

• エントリーDOI: 10.2210/pdb2qts/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Acid-sensing ion channel, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: acid-sensing, ion channel, trimer, membrane protein
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 304818.62

構造登録者

Jasti, J.,Furukawa, H.,Gonzales, E.B.,Gouaux, E. (登録日: 2007-08-02, 公開日: 2007-09-25, 最終更新日: 2024-10-30)

主引用文献

Jasti, J.,Furukawa, H.,Gonzales, E.B.,Gouaux, E.
Structure of acid-sensing ion channel 1 at 1.9A resolution and low pH
Nature, 449:316-323, 2007

PubMed Abstract: Acid-sensing ion channels (ASICs) are voltage-independent, proton-activated receptors that belong to the epithelial sodium channel/degenerin family of ion channels and are implicated in perception of pain, ischaemic stroke, mechanosensation, learning and memory. Here we report the low-pH crystal structure of a chicken ASIC1 deletion mutant at 1.9 A resolution. Each subunit of the chalice-shaped homotrimer is composed of short amino and carboxy termini, two transmembrane helices, a bound chloride ion and a disulphide-rich, multidomain extracellular region enriched in acidic residues and carboxyl-carboxylate pairs within 3 A, suggesting that at least one carboxyl group bears a proton. Electrophysiological studies on aspartate-to-asparagine mutants confirm that these carboxyl-carboxylate pairs participate in proton sensing. Between the acidic residues and the transmembrane pore lies a disulphide-rich 'thumb' domain poised to couple the binding of protons to the opening of the ion channel, thus demonstrating that proton activation involves long-range conformational changes.

PubMed: 17882215
DOI: 10.1038/nature06163

実験手法

X-RAY DIFFRACTION (1.9 Å)