FIGURE

Fig. 2

ID

ZDB-FIG-230319-29

Publication

Gibbs et al., 2023 - Conformational transitions and allosteric modulation in a heteromeric glycine receptor

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Fig. 2

Conformational changes within the αβGlyR pore in response to different ligands.

A Map and model representations of M2 helices in the αB and β subunits as seen in αβGly-Stry, αβGly-Gly and αβGly-Gly-Ivm (σ = 0.146, 0.25, and 0.13, respectively). The ion permeation profiles of the channel pore were generated using HOLE⁸⁵. The side chains lining the constrictions (green dots) are labeled. B The smallest pore radii as a function of the position along the pore axis. The radius of a hydrated chloride ion is indicated as a dotted line and shows that all three states are expected to be non-conducting, though this analysis does not consider hydrophobicity or pore asymmetry. Residues lining the M2 helix for each subunit are shown below the plot. C Top-down views of the L9′ and P-2′ positions which respectively correspond to the channel activation and desensitization gates. Distance labels are in Å.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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