View source for 9oqg


==Human pannexin 1 channel with 0 mM ATP==
<StructureSection load='9oqg' size='340' side='right'caption='[[9oqg]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9oqg]] 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=9OQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OQG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.58&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9oqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oqg OCA], [https://pdbe.org/9oqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oqg RCSB], [https://www.ebi.ac.uk/pdbsum/9oqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oqg ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9oqg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Du J]]
[[Category: Li Y]]
[[Category: Lu W]]
[[Category: Ruan Z]]