Fig. 2: High-resolution details of GYKI-52466 binding.
From: Allosteric competition and inhibition in AMPA receptors
a, GYKI-52466 (pink, carbon; blue, nitrogen; red, oxygen) makes extensive contacts with residues within the TMD collar region (orange ribbons), including Ser615 on the neighboring M4 helix counterclockwise from the ‘bound’ subunit (purple). b, Schematic representation of the interactions between GYKI-52466 and TMD collar residues. The TM helix that each residue comes from is labeled below each residue. The π bonds are represented by curved lines; van der Waals interactions are represented by dashes. Carbon, nitrogen and oxygen atoms are colored according to a. c, Top-down view of the inhibited TMD, showing landmark residues based on the GYKI-52466-binding site. d, Plot detailing the inter-residue distances between landmark GYKI-52466-binding pocket residues and the solvent-accessible surface surrounding GYKI-52466.
