FIGURE

Fig. 2

ID

ZDB-FIG-200910-6

Publication

Kumar et al., 2020 - Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs

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Fig. 2

Conformational changes underlying GlyR gating.

a Cryo-EM density segments for neurotransmitter binding site residues and glycine ligand as seen in the GlyR–Gly structure. Residues in the principal subunit and complementary subunit are indicated in black and magenta, respectively. b LigPlot analysis of glycine orientation in the binding pocket and residues within 4 Å distance are displayed in red⁷⁰. c Comparison of the neurotransmitter binding site for the GlyR–Apo and GlyR–Gly conformations. The residues that are involved in neurotransmitter binding are shown in sticks. d Cryo-EM map showing the density for M2 and PTX bound in the pore of GlyR–Gly/PTX. The interacting residues are shown in stick representation. For clarity, M2 for only two diagonal subunits are shown. e LigPlot analysis of PTX and the interacting residues. f A close-up of the M2 conformations is shown upon aligning the three GlyR conformations. Positions Leu9′ and Pro-2′ are shown as sticks.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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