Structural mechanism of glutamate receptor activation and desensitization

• Published in: Nature (London) Vol. 514; no. 7522; pp. 328 - 334
• Main Authors: Meyerson, Joel R., Kumar, Janesh, Chittori, Sagar, Rao, Prashant, Pierson, Jason, Bartesaghi, Alberto, Mayer, Mark L., Subramaniam, Sriram
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 16.10.2014; Nature Publishing Group
• Subjects: 101/28; 147/28; 631/378/2586; 631/535/1258; Amino acids; Analysis; Animals; Binding Sites; Cell receptors; Cryoelectron Microscopy; Crystal structure; GluK2 Kainate Receptor; Glutamic Acid - chemistry; Glutamic Acid - metabolism; Glutamic Acid - pharmacology; Humanities and Social Sciences; Ion Channel Gating - drug effects; Ligands; Models, Molecular; multidisciplinary; Nervous system; Physiological aspects; Protein Structure, Tertiary - drug effects; Rats; Receptors, AMPA - antagonists & inhibitors; Receptors, AMPA - chemistry; Receptors, AMPA - metabolism; Receptors, AMPA - ultrastructure; Receptors, Kainic Acid - chemistry; Receptors, Kainic Acid - metabolism; Receptors, Kainic Acid - ultrastructure; Science; Studies; Symmetry; United States

Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion flux across the membrane, we trapped rat AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)...