2qts

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 2qts, resolution 1.900Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with , and as ligands. 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 Wed Jan 23 13:08:26 2008