andtheirresponsestoglutamateandglycine(A)(i)Cartoon.pptVIP

Chimaeric NMDARs and their responses to glutamate and glycine A i Cartoon sketch of the tetrameric nature of an ionotropic NMDAR and the linear protein structure, ii of an NMDAR subunit together with a cartoon depiction of its tertiary structure, iii... Timothy OLeary, and David?J.A. Wyllie Biochm. Soc. Trans. 2009;37:1347-1354 ?2009 by Portland Press Ltd Chimaeric NMDARs and their responses to glutamate and glycine A i Cartoon sketch of the tetrameric nature of an ionotropic NMDAR and the linear protein structure, ii of an NMDAR subunit together with a cartoon depiction of its tertiary structure, iii showing the proposed membrane topology of three membrane-spanning domains M1, M3 and M4 and a re-entrant loop M2 and the location of the NTD and CTD. The LBD is formed by the S1 and S2 regions of the protein, which come together to form a hinged clamshell-like structure. B Cartoon depiction of wild-type WT and chimaeric GluN2A and GluN2D subunits showing how the various functional domains from the GluN2D subunit are incorporated into the GluN2A subunit. C Mean glutamate concentration–response curves for GluN2A 2D-M1M2M3 and GluN2A 2D-S1M1M2M3S2 NMDAR constructs. Inclusion of the M1, M2 and M3 domains from the GluN2D subunit in GluN2A subunits does not alter glutamate potency compared with GluN2A WT -containing NMDARs. When S1 and S2 regions are also included, a shift to a GluN2D-like potency is observed. D Mean glycine concentration–response curves for GluN2A 2D-M1M2M3 and GluN2A 2D-S1M1M2M3S2 constructs. Inclusion of the M1, M2 and M3 domains from the GluN2D subunit in GluN2A subunits does not alter glycine potency compared with GluN2A WT -containing NMDARs. When S1 and S2 regions are also included a shift to a more GluN2D-like potency is observed. C and D are reproduced from [18] with permission.