Molecular Sites for the Positive Allosteric Modulation of Glycine Receptors by Endocannabinoids
Figure 7
The positive allosteric modulation elicited by NA-Gly is influenced by a conserved lysine residue within the α1 GlyR large intracellular loop.
(A) The schematic receptor representation and the primary sequence alignment describe the position of the conserved intracellular K385 residue within the GlyR structure (B) Glycine-activated current traces from wild-type or K385A-mutated α1 GlyRs before (black) and during the application of NA-Gly (5 µM, red) (C) Concentration-response curves for NA-Gly obtained from wild-type and K385-mutated GlyRs. The intracellular mutation significantly attenuated the NA-Gly-induced potentiation of α1 GlyRs.