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| {{STRUCTURE_2qts| PDB=2qts | SCENE= }} | | {{STRUCTURE_2qts| PDB=2qts | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17882215}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17882215 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17882215}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| [[Category: Trimer]] | | [[Category: Trimer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:40:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:47:49 2008'' |
