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A DFT approach to discriminate the antagonist and partial agonist activity of ligands binding to the NMDA receptor
Published in Molecular Physics, 2018
Zeynep Pinar Haslak, Esra Bozkurt, Bercem Dutagaci, Frank De Proft, Viktorya Aviyente, Freija De Vleeschouwer
Ionotropic glutamate receptors (iGluRs) are located at the membranes of neuronal cells and play key roles in synaptic plasticity. Monomers of iGluRs contain an extracellular N terminal domain (NTD), an intracellular C terminal domain (CTD), three transmembrane domains (M1, M2 and M3), a re-entrant membrane loop (P-loop) and a ligand binding domain (LBD) [1]. iGluRs act as cation-selective ion channels upon binding of agonists to their LBDs. They can be classified into three main groups with respect to the affinities of specific agonists N-methyl-D-aspartate (NMDA), kainic acid (KA) and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) [2].