Fig. 4: Allosteric competition in AMPARs.
From: Allosteric competition and inhibition in AMPA receptors
a, Local LBD clamshell from the allosterically inhibited state (GluA2-γ2IS-1) with landmark residues to show D1 and D2 separation within the dimer. This represents the dimer during negative allosteric modulation. b, Local LBD clamshell dimer activated in the presence of CTZ (PDB 5WEO), showing decreased D1 separation and increased D2 separation. This is indicative of positive allosteric modulation. CTZ is shown in blue. Distances were measured as in Fig. 3. c, Top-down view of the LBD layer in GluA2-γ2IS-1 with Leu467, where the Leu467Cys substitution is used for maleimide dye labeling, marked with a blue sphere, and intersubunit Leu467–Leu467 Cα distances are labeled. d, Plot of FRET efficiency between LBD clamshells within a local dimer when GluA2-γ2FRET was treated with 1 mM Glu + 100 μM CTZ alone versus 1 mM Glu + 100 μM GYKI-52466. e, Same as in d but with GluA2FRET. Data are represented as the mean values ± s.e.m. across multiple days. The number of molecules included in the analysis for each condition is as follows: GluA2-γ2FRET (CTZ, n = 76; GYKI-52466, n = 77) and GluA2FRET (CTZ, n = 62*; GYKI-52466, n = 96). *In this case, 30 molecules with 1 mM Glu and 100 μM CTZ were obtained from Carrillo et al.60.
