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- W4383218181 abstract "Gap junction channels (GJCs) mediate intercellular communication by connecting two neighboring cells and enabling direct exchange of ions and small molecules. Cell coupling via connexin-43 (Cx43) GJCs is important in a wide range of cellular processes in health and disease -, yet the structural basis of Cx43 function and regulation has not been determined until now. Here we describe the structure of a human Cx43 GJC solved by cryo-EM and single particle analysis at 2.26 Å resolution. The pore region of Cx43 GJC features several lipid-like densities per Cx43 monomer, located close to a putative lateral access site at the monomer boundary. We found a previously undescribed conformation on the cytosolic side of the pore, formed by the N-terminal domain and the transmembrane helix 2 of Cx43 and stabilized by a small molecule. Structures of the Cx43 GJC and hemichannels in nanodiscs reveal a similar gate arrangement. The features of the Cx43 GJC and hemichannel cryo-EM maps and the channel properties revealed by molecular dynamics simulations suggest that the captured states of Cx43 are consistent with a closed state." @default.
- W4383218181 created "2023-07-06" @default.
- W4383218181 date "2023-07-05" @default.
- W4383218181 modified "2023-09-27" @default.
- W4383218181 title "Reviewer #1 (Public Review): Structure of the connexin-43 gap junction channel in a putative closed state" @default.
- W4383218181 doi "https://doi.org/10.7554/elife.87616.2.sa1" @default.
- W4383218181 hasPublicationYear "2023" @default.
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