2qts

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:35, 30 October 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2qts.png|left|200px]]
 
-
{{STRUCTURE_2qts| PDB=2qts | SCENE= }}
+
==Structure of an acid-sensing ion channel 1 at 1.9 A resolution and low pH==
 +
<StructureSection load='2qts' size='340' side='right'caption='[[2qts]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
 +
</table>
 +
== 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>
-
{{ABSTRACT_PUBMED_17882215}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2qts" style="background-color:#fffaf0;"></div>
-
[[2qts]] is a 6 chain structure with 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].
+
==See Also==
==See Also==
-
*[[Ion channels|Ion channels]]
+
*[[Ion channels 3D structures|Ion channels 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:017882215</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Furukawa, H.]]
+
[[Category: Large Structures]]
-
[[Category: Gonzales, E B.]]
+
[[Category: Furukawa H]]
-
[[Category: Gouaux, E.]]
+
[[Category: Gonzales EB]]
-
[[Category: Jasti, J.]]
+
[[Category: Gouaux E]]
-
[[Category: Acid-sensing]]
+
[[Category: Jasti J]]
-
[[Category: Ion channel]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Trimer]]
+

Current revision

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

PDB ID 2qts

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qts"
Personal tools