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. Author manuscript; available in PMC: 2021 Dec 22.
Published in final edited form as: Neuropharmacology. 2021 May 31;194:108624. doi: 10.1016/j.neuropharm.2021.108624

Figure 5. Possible mechanism of positive allostery of DNRAbs on GluN2A-containing NMDARs.

Figure 5.

(A) Individual domains within a GluN2A subunit. DWEYS is a mimetope of dsDNA and is the major binding site for DNRAbs. Model structure of 4TLM (Amin et al., 2017).

(B) Zn2+ acts as a negative allosteric modulator of GluN2A-containing NMDARs by inducing clam-shell closure of the ATD. The DWEYS motif is at the hinge of the ATD clam-shell and DNRAb binding may potentiate currents by forcing open the clam-shell.

Synaptic currents recorded from a CA1 pyramidal neuron with Schaffer collateral stimulation. Currents recorded at −70 mV in a solution containing no added Mg2+ (LPW, unpublished data).