Faculty, Staff and Student Publications
Publication Date
8-1-2024
Journal
Current Opinion in Structural Biology
DOI
10.1016/j.sbi.2024.102833
PMID
38733862
PMCID
PMC11283939
PubMedCentral® Posted Date
8-1-2025
PubMedCentral® Full Text Version
Author MSS
Abstract
The ionotropic glutamate receptors (iGluRs) are comprised of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA), N-methyl-d-aspartate receptor, kainate, and delta subtypes and are pivotal in neuronal plasticity. Recent structural studies on AMPA receptors reveal intricate conformational changes during activation and desensitization elucidating the steps from agonist binding to channel opening and desensitization. Additionally, interactions with auxiliary subunits, including transmembrane AMPA-receptor regulatory proteins, germ-cell-specific gene 1-like protein, and cornichon homologs, intricately modulate AMPA receptors. We discuss the recent high-resolution structures of these complexes that unveil stoichiometry, subunit positioning, and differences in specific side-chain interactions that influence these functional modulations.
Keywords
Receptors, AMPA, Humans, Animals, Ion Channel Gating, Protein Conformation, Protein Subunits, Models, Molecular, Activation, Cryo-EM, Dynamics, Glutamate receptors, Transmembrane AMPA-receptor regulatory protein (TARP), α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)
Published Open-Access
yes
Recommended Citation
Cuauhtemoc U Gonzalez and Vasanthi Jayaraman, "Structural Dynamics in α-Amino-3-Hydroxy-5-Methyl-4-Isoxazole Propionic Acid Receptor Gating" (2024). Faculty, Staff and Student Publications. 4530.
https://digitalcommons.library.tmc.edu/uthgsbs_docs/4530
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