The pore domain in glutamate-gated ion channels: Structure, drug binding and similarity with potassium channels

• Published in: Biochimica et biophysica acta. Biomembranes Vol. 1862; no. 10; p. 183401
• Main Authors: Tikhonov, Denis B., Zhorov, Boris S.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2020
• Subjects: Amino Acid Sequence; AMPA channels; Channel block; Cryo-EM structures; Cryoelectron Microscopy; Crystal structures; Glutamic Acid - physiology; Ion Channel Gating - physiology; Ionotropic glutamate receptors; Molecular modeling; NMDA channels; Potassium Channels - chemistry; Potassium Channels - metabolism; Protein Conformation; Sequence Homology, Amino Acid; Crystal structures; iGluR; AMPA; NMDA channels; Ionotropic glutamate receptors; AMPAR; Channel block; PDB; AMPA channels; Cryo-EM structures; Molecular modeling; NMDA; NMDAR

Ionotropic glutamate receptors in the CNS excitatory synapses of vertebrates are involved in numerous physiological and pathological processes. Decades of intensive studies greatly advanced our understanding of molecular organization of these transmembrane proteins. Here we focus on the channel pore...