2qts
From Proteopedia
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, resolution 1.900Å | |||||||
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Ligands: | , and | ||||||
Gene: | ACCN2 (Gallus gallus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH
Overview
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.
About this Structure
2QTS is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH., Jasti J, Furukawa H, Gonzales EB, Gouaux E, Nature. 2007 Sep 20;449(7160):316-23. PMID:17882215
Page seeded by OCA on Thu Mar 20 18:29:32 2008
Categories: Gallus gallus | Single protein | Furukawa, H. | Gonzales, E B. | Gouaux, E. | Jasti, J. | CL | MAL | NAG | Acid-sensing | Ion channel | Membrane protein | Trimer