Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors

Abstract

Background: NMDA receptor deactivation is characteristically slow and depends on unique intersubunit contacts in the ligand binding domain. Results: These additional contacts slow current deactivation mainly by increasing gating. Conclusion: Slow deactivation reflects higher open probability due to more stable heterodimers. Significance: A firmer heterodimer interface supports basic functional differences between NMDA and non-NMDA glutamate-gated channels.