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2qts

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[[Image:2qts.jpg|left|200px]]
[[Image:2qts.jpg|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|GENE= ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
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{{STRUCTURE_2qts| PDB=2qts | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qts OCA], [http://www.ebi.ac.uk/pdbsum/2qts PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qts RCSB]</span>
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'''Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH'''
'''Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH'''
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[[Category: Gouaux, E.]]
[[Category: Gouaux, E.]]
[[Category: Jasti, J.]]
[[Category: Jasti, J.]]
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[[Category: acid-sensing]]
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[[Category: Acid-sensing]]
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[[Category: ion channel]]
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[[Category: Ion channel]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: trimer]]
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[[Category: Trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:40:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:13 2008''
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Revision as of 12:40, 4 May 2008

Template:STRUCTURE 2qts

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 Sun May 4 15:40:06 2008

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