Fig. 2: Common hydrophobic binding site of MFQ and AA in Cx36 GJC. | Nature Communications

Fig. 2: Common hydrophobic binding site of MFQ and AA in Cx36 GJC.

From: Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer

Fig. 2

a–d The ribbon representation of Cx36Nano-BL-WT in PLN (a yellow ribbon), Cx36Nano-BL-MFQ (b green ribbon), Cx36Nano-BL-AA (c pink ribbon), and their superimposition (d). The close-up of the H.G. is presented in boxes. The H.G. is composed of hydrophobic residues from TM1 (Ile35, Val38, and Ala39) and TM2 (Val80, Ile83, and Ile84). The NTH and Trp4 of Cx36Nano-BL-WT in PLN are colored in magenta. H.G.-bound MFQ and AA, along with their coulomb density maps, are shown in cyan, brown, and gray, respectively. H.G. hydrophobic groove, NTH N-terminal helix, PLN pore-lining NTH, FN flexible NTH, MFQ mefloquine, AA arachidonic acid.

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