7f8j: Difference between revisions
New page: '''Unreleased structure''' The entry 7f8j is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Cryo-EM structure of human pannexin-1 in a nanodisc== | |||
<StructureSection load='7f8j' size='340' side='right'caption='[[7f8j]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7f8j]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F8J 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=7f8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f8j OCA], [https://pdbe.org/7f8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f8j RCSB], [https://www.ebi.ac.uk/pdbsum/7f8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f8j 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 7f8j" 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]] | |||
Latest revision as of 11:38, 23 February 2022
Cryo-EM structure of human pannexin-1 in a nanodiscCryo-EM structure of human pannexin-1 in a nanodisc
Structural highlights
Function[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.[1] [2] Publication Abstract from PubMedPannexin (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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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