MEDIA

Morph video showing conformational changes in GluN1/3A receptors

Video is published under a Creative Commons Attribution 4.0 International License from Kim, J., Benton, A.J., Lotti, J.S. et al. Structural and mechanistic insights into gating and allosteric modulation of GluN1–GluN3A NMDA receptors. Nat Struct Mol Biol 33, 1299–1310 (2026). https://doi.org/10.1038/s41594-026-01866-9

9/13/2026

Quad-barrel piezo-driven fast solution exchange for patch-clamp electrophysiology

Demonstration of sub-millisecond solution exchange using piezo-driven translation of a custom-made quad-barrel perfusion system. The video and perfusion system were made in the Hansen lab by Samuel Galindo.

11/7/2025

Ligand binding to wild type and mutant GluN1 agonist binding domains

Representative molecular dynamics simulations from Rouzbeh et al., J Gen Physiol, 2023. In these simulations, the binding of glycine and the GluN1-selective competitive antagonists, CGP-78608 and L-689,560, is evaluated in the isolated agonist binding domain of the NMDA receptor subunit GluN1 with and without mutations in the binding site (FA+TL or FH+RK) that are known to abolish glycine binding.

1/23/2023

GluN1 ABD with glycine

Glycine is stably bound to wild type GluN1.

GluN1FA+TL ABD with glycine

Glycine readily unbinds from mutant GluN1FA+TL.

GluN1 ABD with CGP-78608

CGP-78608 is stably bound to wild type GluN1.

GluN1FA+TL ABD with CGP-78608

CGP-78608 unbinds from mutant GluN1FA+TL.

GluN1FH+RK ABD with CGP-78608

CGP-78608 remains partially bound to mutant GluN1FH+RK.

GluN1 ABD with L-689,560

L-689,560 is stably bound to wild type GluN1.

GluN1FA+TL ABD with L-689,560

L-689,560 is stably bound to mutant GluN1FA+TL.

GluN1FH+RK ABD with L-689,560

L-689,560 unbinds from mutant GluN1FH+RK.

Ligand binding to the glycine site in the GluN1 agonist binding domain

Representative molecular dynamics simulations from Rouzbeh et al., J Gen Physiol, 2023. These simulations suggest that binding of glycine and the GluN1-selective competitive antagonists, CGP-78608 and L-689,560, promotes distinct conformations of the GluN1 NMDA receptor agonist binding domain.

1/23/2023

GluN1 ABD with glycine

Molecular dynamics simulation (2500 ns) of glycine bound to the GluN1 NMDA receptor agonist binding domain.

GluN1 ABD with CGP-78608

Molecular dynamics simulation (2500 ns) of CGP-78608 bound to the GluN1 NMDA receptor agonist binding domain.

GluN1 ABD with L-689,560

Molecular dynamics simulation (2500 ns) of L-689,560 bound to the GluN1 NMDA receptor agonist binding domain.