4nty: Difference between revisions
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<StructureSection load='4nty' size='340' side='right'caption='[[4nty]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='4nty' size='340' side='right'caption='[[4nty]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nty]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4nty]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Micrurus_tener_tener Micrurus tener tener]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NTY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</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=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</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=4nty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nty OCA], [https://pdbe.org/4nty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nty RCSB], [https://www.ebi.ac.uk/pdbsum/4nty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nty ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ion channels 3D structures|Ion channels 3D structures]] | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
*[[Phospholipase A2 homolog|Phospholipase A2 homolog]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Micrurus tener tener]] | ||
[[Category: Baconguis | [[Category: Baconguis I]] | ||
[[Category: Bohlen | [[Category: Bohlen CJ]] | ||
[[Category: Goehring | [[Category: Goehring A]] | ||
[[Category: Gouaux | [[Category: Gouaux E]] | ||
[[Category: Julius | [[Category: Julius D]] | ||
Latest revision as of 06:20, 21 November 2024
Cesium sites in the crystal structure of acid-sensing ion channel in complex with snake toxinCesium sites in the crystal structure of acid-sensing ion channel in complex with snake toxin
Structural highlights
FunctionASIC1_CHICK Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).[1] Publication Abstract from PubMedAcid-sensing ion channels (ASICs) detect extracellular protons produced during inflammation or ischemic injury and belong to the superfamily of degenerin/epithelial sodium channels. Here, we determine the cocrystal structure of chicken ASIC1a with MitTx, a pain-inducing toxin from the Texas coral snake, to define the structure of the open state of ASIC1a. In the MitTx-bound open state and in the previously determined low-pH desensitized state, TM2 is a discontinuous alpha helix in which the Gly-Ala-Ser selectivity filter adopts an extended, belt-like conformation, swapping the cytoplasmic one-third of TM2 with an adjacent subunit. Gly 443 residues of the selectivity filter provide a ring of three carbonyl oxygen atoms with a radius of approximately 3.6 A, presenting an energetic barrier for hydrated ions. The ASIC1a-MitTx complex illuminates the mechanism of MitTx action, defines the structure of the selectivity filter of voltage-independent, sodium-selective ion channels, and captures the open state of an ASIC. X-ray structure of Acid-sensing ion channel 1-snake toxin complex reveals open state of a na(+)-selective channel.,Baconguis I, Bohlen CJ, Goehring A, Julius D, Gouaux E Cell. 2014 Feb 13;156(4):717-29. doi: 10.1016/j.cell.2014.01.011. Epub 2014 Feb, 6. PMID:24507937[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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