Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain

Ionotropic glutamate receptors (iGluRs) mediate the majority of excitatory neurotransmission in the brain. Their dysfunction is implicated in many neurological disorders, rendering iGluRs potential drug targets. Here, we performed a systematic analysis of the druggability of two major iGluR subfamil...

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Veröffentlicht in:	Structure (London) 2019-02, Vol.27 (2), p.241-252.e3
Hauptverfasser:	Lee, Ji Young, Krieger, James, Herguedas, Beatriz, García-Nafría, Javier, Dutta, Anindita, Shaikh, Saher A., Greger, Ingo H., Bahar, Ivet
Format:	Artikel
Sprache:	eng
Schlagworte:	allosteric interactions Allosteric Site AMPA Binding Sites Crystallography, X-Ray Drug Evaluation, Preclinical druggability simulations GluA3 N-terminal domain HEK293 Cells Humans ionotropic glutamate receptors kainate receptors ligand binding Ligands molecular dynamics Molecular Dynamics Simulation NMDA Protein Binding Protein Conformation Protein Domains protein-protein interface Receptors, AMPA - agonists Receptors, AMPA - chemistry Receptors, AMPA - metabolism
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