2qts: Difference between revisions
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[[Image:2qts.jpg|left|200px]] | [[Image:2qts.jpg|left|200px]] | ||
'''Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH''' | {{Structure | ||
|PDB= 2qts |SIZE=350|CAPTION= <scene name='initialview01'>2qts</scene>, resolution 1.900Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |||
}} | |||
'''Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2QTS is a [ | 2QTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QTS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17882215 17882215] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:29:32 2008'' | ||
Revision as of 16:29, 20 March 2008
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| 2qts, resolution 1.900Å | |||||||||||||
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| Ligands: | MAL, NAG and CL | ||||||||||||
| 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
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