2qts
From Proteopedia
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|PDB= 2qts |SIZE=350|CAPTION= <scene name='initialview01'>2qts</scene>, resolution 1.900Å | |PDB= 2qts |SIZE=350|CAPTION= <scene name='initialview01'>2qts</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |GENE= ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Gouaux, E.]] | [[Category: Gouaux, E.]] | ||
[[Category: Jasti, J.]] | [[Category: Jasti, J.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MAL]] | ||
| - | [[Category: NAG]] | ||
[[Category: acid-sensing]] | [[Category: acid-sensing]] | ||
[[Category: ion channel]] | [[Category: ion channel]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:13 2008'' |
Revision as of 01:53, 31 March 2008
| |||||||
| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | ACCN2 (Gallus gallus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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