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7f8n
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7f8n is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Human pannexin-1 showing a conformational change in the N-terminal domain and blocked pore== | |
| + | <StructureSection load='7f8n' size='340' side='right'caption='[[7f8n]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7f8n]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F8N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</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=7f8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f8n OCA], [https://pdbe.org/7f8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f8n RCSB], [https://www.ebi.ac.uk/pdbsum/7f8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f8n 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 == | ||
| + | Pannexin (PANX) family proteins form large-pore channels that mediate purinergic signaling. We analyzed the cryo-EM structures of human PANX1 in lipid nanodiscs to elucidate the gating mechanism and its regulation by the amino terminus in phospholipids. The wild-type channel has an amino-terminal funnel in the pore, but in the presence of the inhibitor probenecid, a cytoplasmically oriented amino terminus and phospholipids obstruct the pore. Functional analysis using whole-cell patch-clamp and oocyte voltage clamp showed that PANX1 lacking the amino terminus did not open and had a dominant negative effect on channel activity, thus confirming that the amino-terminal domain played an essential role in channel opening. These observations suggest that dynamic conformational changes in the amino terminus of human PANX1 are associated with lipid movement in and out of the pore. Moreover, the data provide insight into the gating mechanism of PANX1 and, more broadly, other large-pore channels. | ||
| - | + | Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids.,Kuzuya M, Hirano H, Hayashida K, Watanabe M, Kobayashi K, Terada T, Mahmood MI, Tama F, Tani K, Fujiyoshi Y, Oshima A Sci Signal. 2022 Feb 8;15(720):eabg6941. doi: 10.1126/scisignal.abg6941. Epub, 2022 Feb 8. PMID:35133866<ref>PMID:35133866</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7f8n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fujiyoshi, Y]] | ||
| + | [[Category: Hayashida, K]] | ||
| + | [[Category: Hirano, H]] | ||
| + | [[Category: Kobayashi, K]] | ||
| + | [[Category: Kuzuya, M]] | ||
| + | [[Category: Oshima, A]] | ||
| + | [[Category: Tani, K]] | ||
| + | [[Category: Watanabe, M]] | ||
| + | [[Category: Atp release channel]] | ||
| + | [[Category: Transport protein]] | ||
| + | [[Category: Vertebrate innexin homolog]] | ||
Current revision
Human pannexin-1 showing a conformational change in the N-terminal domain and blocked pore
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