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9oqm

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m (Protected "9oqm" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 9oqm is ON HOLD
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==Apo class from combined 0, 10, 20, 30 mM ATP datastes==
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<StructureSection load='9oqm' size='340' side='right'caption='[[9oqm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9oqm]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OQM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9oqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oqm OCA], [https://pdbe.org/9oqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oqm RCSB], [https://www.ebi.ac.uk/pdbsum/9oqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oqm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PANX1_HUMAN PANX1_HUMAN] Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis.<ref>PMID:16908669</ref> <ref>PMID:20829356</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Purinergic signaling relies on ATP release through exocytosis and large-pore channels. Large-pore channels permeate both small anions like chloride and large signaling molecules like ATP, but how this broad cargo selectivity is structurally controlled remains elusive. Here we investigate PANX1, a prototypical large-pore channel, and uncover structural plasticity at the extracellular entrance formed by seven tryptophan (W74) residues. The W74 sidechains are flexible, sampling conformations that range from a constricted state permissive only to chloride to a dilated state compatible with ATP. These states are coupled to variable cation-pi interactions between W74 and arginine 75 (R75), suggesting a mechanism for dynamic tuning of pore architecture and selective cargo permeation. We also identify mefloquine as a positive modulator of PANX1 that binds near the side tunnel to control ion flow through this pathway. Together, these findings define the structural principles underlying PANX1 permeation and modulation.
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Authors:
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Structural basis of PANX1 permeation and positive modulation by mefloquine.,Li Y, Ruan Z, Lee J, Orozco IJ, Zhou E, Du J, Lu W Nat Commun. 2025 Dec 11;16(1):11057. doi: 10.1038/s41467-025-66028-9. PMID:41381453<ref>PMID:41381453</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9oqm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Du J]]
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[[Category: Li Y]]
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[[Category: Lu W]]
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[[Category: Ruan Z]]

Current revision

Apo class from combined 0, 10, 20, 30 mM ATP datastes

PDB ID 9oqm

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