Fig. 3: Propagation of glycine-induced structural changes.
From: Asymmetric gating of a human hetero-pentameric glycine receptor
a–c Overlay of all 5 glycine binding pockets in each of the gly-1(open) (a), gly-2 (expanded open) (b) and gly-3(desensitized) (c) states, with (+) and (−) sides indicated. The key amino acids for glycine binding are shown. d Dose response of glycine for α (+) (α1emF207Aβem), α(+) (α1emR65Dβem), β(+) side (α1emβemY231A), β(−) side (α1emβemR86T) and β double sides (α1emβemR86TY231A) mutants. Data are represented as mean ± SEM (n = 9 cells for α1emF207Aβem, n = 8 cells for (α1em+ α1em)F207Aβem, n = 9 cells for α1emR65Dβem, n = 7 cells for (α1em + α1emR65D)βem, n = 6 cells for α1emβemY231A, n = 7 cells α1emβemR86T, for n = 8 cells for α1emβemR86TY231A). EC50 from Hill fits are listed. Source data are provided as a Source Data file. e–g The orthosteric pocket changes from apo state to gly-1(open), gly-2(expanded open) and gly-3(desensitized) states at α.D(+)β(−) (e), β(+)α.A(−) (f) and α.A(+)α.B(−) (g) subunit interfaces. The key amino acids are indicated. h Superimposition of individual subunits in the apo (α: white, β: gray) and gly-1(open) states (α: blue, β: salmon). The rotational motion of ECD propagates to TMD in different ways. Arrows indicate the direction of motion. Green rectangles represent the pore axis.
