6uzy
From Proteopedia
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<StructureSection load='6uzy' size='340' side='right'caption='[[6uzy]], [[Resolution|resolution]] 3.38Å' scene=''> | <StructureSection load='6uzy' size='340' side='right'caption='[[6uzy]], [[Resolution|resolution]] 3.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6uzy]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UZY OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6uzy]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UZY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UZY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=R16:HEXADECANE'>R16</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=R16:HEXADECANE'>R16</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">panx1, LOC100170473, PANX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Silurana (Xenopus) tropicalis])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uzy OCA], [http://pdbe.org/6uzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uzy RCSB], [http://www.ebi.ac.uk/pdbsum/6uzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uzy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/B3DLA5_XENTR B3DLA5_XENTR]] Structural component of the gap junctions and the hemichannels.[RuleBase:RU010713] | [[http://www.uniprot.org/uniprot/B3DLA5_XENTR B3DLA5_XENTR]] Structural component of the gap junctions and the hemichannels.[RuleBase:RU010713] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The plasma membrane adenosine triphosphate (ATP) release channel pannexin 1 (PANX1) has been implicated in many physiological and pathophysiological processes associated with purinergic signaling, including cancer progression, apoptotic cell clearance, inflammation, blood pressure regulation, oocyte development, epilepsy and neuropathic pain. Here we present near-atomic-resolution structures of human and frog PANX1 determined by cryo-electron microscopy that revealed a heptameric channel architecture. Compatible with ATP permeation, the transmembrane pore and cytoplasmic vestibule were exceptionally wide. An extracellular tryptophan ring located at the outer pore created a constriction site, potentially functioning as a molecular sieve that restricts the size of permeable substrates. The amino and carboxyl termini, not resolved in the density map, appeared to be structurally dynamic and might contribute to narrowing of the pore during channel gating. In combination with functional characterization, this work elucidates the previously unknown architecture of pannexin channels and establishes a foundation for understanding their unique channel properties. | ||
| + | |||
| + | Cryo-EM structures of the ATP release channel pannexin 1.,Deng Z, He Z, Maksaev G, Bitter RM, Rau M, Fitzpatrick JAJ, Yuan P Nat Struct Mol Biol. 2020 Apr;27(4):373-381. doi: 10.1038/s41594-020-0401-0. Epub, 2020 Mar 30. PMID:32231289<ref>PMID:32231289</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6uzy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:20, 15 April 2020
Cryo-EM structure of Xenopus tropicalis pannexin 1
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