5h1q

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(New page: '''Unreleased structure''' The entry 5h1q is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (07:21, 9 August 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5h1q is ON HOLD
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==C. elegans INX-6 gap junction hemichannel==
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<SX load='5h1q' size='340' side='right' viewer='molstar' caption='[[5h1q]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5h1q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H1Q FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h1q OCA], [https://pdbe.org/5h1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h1q RCSB], [https://www.ebi.ac.uk/pdbsum/5h1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h1q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/INX6_CAEEL INX6_CAEEL] Structural component of the gap junctions.[UniProtKB:O61715]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Innexins, a large protein family comprising invertebrate gap junction channels, play an essential role in nervous system development and electrical synapse formation. Here we report the cryo-electron microscopy structures of Caenorhabditis elegans innexin-6 (INX-6) gap junction channels at atomic resolution. We find that the arrangements of the transmembrane helices and extracellular loops of the INX-6 monomeric structure are highly similar to those of connexin-26 (Cx26), despite the lack of significant sequence similarity. The INX-6 gap junction channel comprises hexadecameric subunits but reveals the N-terminal pore funnel, consistent with Cx26. The helix-rich cytoplasmic loop and C-terminus are intercalated one-by-one through an octameric hemichannel, forming a dome-like entrance that interacts with N-terminal loops in the pore. These observations suggest that the INX-6 cytoplasmic domains are cooperatively associated with the N-terminal funnel conformation, and an essential linkage of the N-terminal with channel activity is presumably preserved across gap junction families.
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Authors:
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Atomic structure of the innexin-6 gap junction channel determined by cryo-EM.,Oshima A, Tani K, Fujiyoshi Y Nat Commun. 2016 Dec 1;7:13681. doi: 10.1038/ncomms13681. PMID:27905396<ref>PMID:27905396</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5h1q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Caenorhabditis elegans]]
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[[Category: Large Structures]]
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[[Category: Fujiyoshi Y]]
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[[Category: Oshima A]]
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[[Category: Tani K]]

Current revision

C. elegans INX-6 gap junction hemichannel

5h1q, resolution 3.30Å

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