Figure 4: Molecular details of subunit-specific gephyrin interactions.
From: Molecular basis of the alternative recruitment of GABAA versus glycine receptors through gephyrin
Close up view of the interactions between GephE with (a) GABAAR α3 wild-type-derived peptide (PDB-ID 4TK1), (b) α11SL peptide (PDB-ID 4TK3) and (c,d) GlyR β-derived peptides (PDB-ID 2FTS10 and 4PD1 (ref. 22)) as well as (e) a superposition and (f,g) schematic 2D representations of the GlyR β wild-type and GABAAR α3 wild-type interactions. In a–d, residues mediating the interactions are highlighted in stick representation and are numbered (coloured for the peptides, black for GephE). GephE residues located in subdomain III are coloured in yellow, residues from subdomain IV in marine blue and GephE residues derived from the other subdomain IV′ in cyan. Hydrogen bonds are shown as dotted red lines. Note that the N-terminal-binding motifs engage in conserved interactions, whereas the C-terminal halves interact differentially with GephE.
