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

Oleh:

Jasti, Jayasankar ; Hiroyasu Furukawa ; Gonzales, Eric B. ; Gouaux, Eric

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: NATURE (keterangan: ada di Proquest) vol. 449 no. 7160 (Sep. 2007), page 316.

Ketersediaan

Perpustakaan FK Nomor Panggil: N01.K.2007.09 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

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 Å 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 Å, 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.

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