8f7c
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of human pannexin 2== | |
| + | <StructureSection load='8f7c' size='340' side='right'caption='[[8f7c]], [[Resolution|resolution]] 3.92Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8f7c]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F7C FirstGlance]. <br> | ||
| + | </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=8f7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f7c OCA], [https://pdbe.org/8f7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f7c RCSB], [https://www.ebi.ac.uk/pdbsum/8f7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f7c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://www.uniprot.org/uniprot/PANX2_HUMAN PANX2_HUMAN] Structural component of the gap junctions and the hemichannels. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The pannexin 2 channel (PANX2) participates in multiple physiological processes including skin homeostasis, neuronal development, and ischemia-induced brain injury. However, the molecular basis of PANX2 channel function remains largely unknown. Here, we present a cryo-electron microscopy structure of human PANX2, which reveals pore properties contrasting with those of the intensely studied paralog PANX1. The extracellular selectivity filter, defined by a ring of basic residues, more closely resembles that of the distantly related volume-regulated anion channel (VRAC) LRRC8A, rather than PANX1. Furthermore, we show that PANX2 displays a similar anion permeability sequence as VRAC, and that PANX2 channel activity is inhibited by a commonly used VRAC inhibitor, DCPIB. Thus, the shared channel properties between PANX2 and VRAC may complicate dissection of their cellular functions through pharmacological manipulation. Collectively, our structural and functional analysis provides a framework for development of PANX2-specific reagents that are needed for better understanding of channel physiology and pathophysiology. | ||
| - | + | Structural and functional analysis of human pannexin 2 channel.,He Z, Zhao Y, Rau MJ, Fitzpatrick JAJ, Sah R, Hu H, Yuan P Nat Commun. 2023 Mar 27;14(1):1712. doi: 10.1038/s41467-023-37413-z. PMID:36973289<ref>PMID:36973289</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8f7c" style="background-color:#fffaf0;"></div> |
| - | [[Category: He | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: He Z]] | ||
| + | [[Category: Yuan P]] | ||
Revision as of 06:30, 7 April 2023
Cryo-EM structure of human pannexin 2
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