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- W2557315911 abstract "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." @default.
- W2557315911 created "2016-12-08" @default.
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- W2557315911 date "2016-12-01" @default.
- W2557315911 modified "2023-10-18" @default.
- W2557315911 title "Atomic structure of the innexin-6 gap junction channel determined by cryo-EM" @default.
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- W2557315911 doi "https://doi.org/10.1038/ncomms13681" @default.
- W2557315911 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5146279" @default.
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