Conformational Changes at the Agonist Binding Domain of the N-Methyl-d-Aspartic Acid Receptor

Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor.

The conformational changes in the agonist binding domain of the glycine-binding GluN1 and glutamate-binding GluN2A subunits of the N-methyl D-aspartic acid receptor upon binding agonists of varying efficacy have been investigated by luminescence resonance energy transfer (LRET) measurements. The LRET-based distances indicate a cleft closure conformational change at the GluN1 subunit upon bindin...

N-methyl-D-aspartic acid receptor structure and function.

Paraneoplastic Anti-N-Methyl-D-Aspartic Acid Receptor Encephalitis

N-Hydroxypyrazolyl glycine derivatives as selective N-methyl-D-aspartic acid receptor ligands.

A series of analogues based on N-hydroxypyrazole as a bioisostere for the distal carboxylate group of aspartate have been designed, synthesized, and pharmacologically characterized. Affinity studies on the major glutamate receptor subgroups show that these 4-substituted N-hydroxypyrazol-5-yl glycine (NHP5G) derivatives are selectively recognized by N-methyl- d-aspartic acid (NMDA) receptors and...

Agonist-receptor Interactions and Conformational Changes in the GluR6 Ligand Binding Domain