2qts
From Proteopedia
(New page: 200px<br /><applet load="2qts" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qts, resolution 1.900Å" /> '''Structure of an aci...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Acid-sensing ion channels (ASICs) are voltage-independent, proton-activated receptors that belong to the epithelial sodium | + | 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== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Furukawa, H.]] | [[Category: Furukawa, H.]] | ||
| - | [[Category: Gonzales, E | + | [[Category: Gonzales, E B.]] |
[[Category: Gouaux, E.]] | [[Category: Gouaux, E.]] | ||
[[Category: Jasti, J.]] | [[Category: Jasti, J.]] | ||
| Line 25: | Line 25: | ||
[[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 Thu Feb 21 18:42:12 2008'' |
Revision as of 16:42, 21 February 2008
|
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 Thu Feb 21 18:42:12 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
