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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-09

AUTHORS

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

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 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. More... »

PAGES

316-323

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature06163

DOI

http://dx.doi.org/10.1038/nature06163

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026557001

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17882215


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