3h9v
From Proteopedia
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- | [[Image:3h9v.png|left|200px]] | ||
- | < | + | ==Crystal structure of the ATP-gated P2X4 ion channel in the closed, apo state at 3.1 Angstroms== |
- | + | <StructureSection load='3h9v' size='340' side='right'caption='[[3h9v]], [[Resolution|resolution]] 3.10Å' scene=''> | |
- | + | == Structural highlights == | |
- | or | + | <table><tr><td colspan='2'>[[3h9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H9V 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]] 3.1Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3h9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9v OCA], [https://pdbe.org/3h9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h9v RCSB], [https://www.ebi.ac.uk/pdbsum/3h9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h9v ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/P2X4A_DANRE P2X4A_DANRE] ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium (By similarity). CTP, but not GTP or UTP, functions as a weak affinity agonist for P2RX4 (PubMed:28332633). Activated by extracellularly released ATP, it plays multiple role in immunity and central nervous system physiology (By similarity). Could also function as an ATP-gated cation channel of lysosomal membranes (By similarity).[UniProtKB:P51577][UniProtKB:Q99571][UniProtKB:Q9JJX6]<ref>PMID:28332633</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/h9/3h9v_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=3h9v ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | P2X receptors are cation-selective ion channels gated by extracellular ATP, and are implicated in diverse physiological processes, from synaptic transmission to inflammation to the sensing of taste and pain. Because P2X receptors are not related to other ion channel proteins of known structure, there is at present no molecular foundation for mechanisms of ligand-gating, allosteric modulation and ion permeation. Here we present crystal structures of the zebrafish P2X(4) receptor in its closed, resting state. The chalice-shaped, trimeric receptor is knit together by subunit-subunit contacts implicated in ion channel gating and receptor assembly. Extracellular domains, rich in beta-strands, have large acidic patches that may attract cations, through fenestrations, to vestibules near the ion channel. In the transmembrane pore, the 'gate' is defined by an approximately 8 A slab of protein. We define the location of three non-canonical, intersubunit ATP-binding sites, and suggest that ATP binding promotes subunit rearrangement and ion channel opening. | ||
- | + | Crystal structure of the ATP-gated P2X(4) ion channel in the closed state.,Kawate T, Michel JC, Birdsong WT, Gouaux E Nature. 2009 Jul 30;460(7255):592-8. PMID:19641588<ref>PMID:19641588</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3h9v" style="background-color:#fffaf0;"></div> | |
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- | == | + | |
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==See Also== | ==See Also== | ||
- | *[[Ion channels | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
- | + | *[[Ionotropic receptors|Ionotropic receptors]] | |
- | == | + | == References == |
- | < | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Danio rerio]] | [[Category: Danio rerio]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Gouaux E]] |
- | [[Category: | + | [[Category: Kawate T]] |
- | [[Category: | + | [[Category: Michel JC]] |
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Current revision
Crystal structure of the ATP-gated P2X4 ion channel in the closed, apo state at 3.1 Angstroms
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