Fig. 3: Unique structural features of the Cx36 PLN state. | Nature Communications

Fig. 3: Unique structural features of the Cx36 PLN state.

From: Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel

Fig. 3

ae Detailed structures of NTHs and the NTH-TM1 loops in Cx36 (a), Cx43 (b), Cx46 (c), and Cx50 (d), and their structural alignment (e). fi Ribbon representation of two facing protomers in Cx36 (f), Cx43 (g), Cx46 (h), and Cx50 (i) hemichannel regions. NTHs and acyl chains in the lipid-binding pockets are represented as magenta ribbons and dark gray ball-and-chain models, respectively. The detailed interactions in box 1 (blue dashed line) and box 2 (red dashed line) are represented in the bottom panels. Compared with Cx43, Cx46, and Cx50, Cx36 has two unique structural features: hydrophobic pockets between two NTHs (f, box 1, green dotted circles) and an intermolecular salt bridge between two neighboring NTHs (f, box 2, black dotted line). The Cx36 Glu8, which forms an intermolecular salt bridge by interacting with Arg9, is colored green. Other neighboring protomers and the π-helix are shown as white and black ribbons, respectively.

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