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[[Image:2qts.jpg|left|200px]]


{{Structure
==Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH==
|PDB= 2qts |SIZE=350|CAPTION= <scene name='initialview01'>2qts</scene>, resolution 1.900&Aring;
<StructureSection load='2qts' size='340' side='right'caption='[[2qts]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<table><tr><td colspan='2'>[[2qts]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QTS FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE= ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qts OCA], [https://pdbe.org/2qts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qts RCSB], [https://www.ebi.ac.uk/pdbsum/2qts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qts ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/ASIC1_CHICK ASIC1_CHICK] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).<ref>PMID:16002453</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/2qts_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qts ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH'''
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<ref>PMID:17882215</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qts" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Ion channels 3D structures|Ion channels 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==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://www.ncbi.nlm.nih.gov/pubmed/17882215 17882215]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Furukawa, H.]]
[[Category: Furukawa H]]
[[Category: Gonzales, E B.]]
[[Category: Gonzales EB]]
[[Category: Gouaux, E.]]
[[Category: Gouaux E]]
[[Category: Jasti, J.]]
[[Category: Jasti J]]
[[Category: acid-sensing]]
[[Category: ion channel]]
[[Category: membrane protein]]
[[Category: trimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:13 2008''

Latest revision as of 08:35, 30 October 2024

Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH

2qts, resolution 1.90Å

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