Journal
ANNUAL REVIEW OF PHYSIOLOGY, VOL 75
Volume 75, Issue -, Pages 313-337Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-physiol-030212-183711
Keywords
synaptic transmission; AMPA receptors; kainate receptors; NMDA receptors; crystallography
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Funding
- Intramural NIH HHS [ZIA HD000707-29] Funding Source: Medline
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X-ray crystal structures for the soluble amino-terminal and ligand-binding domains of glutamate receptor ion channels, combined with a 3.6-angstrom-resolution structure of the full-length AMPA receptor GluA2 homotetramer, provide unique insights into the mechanisms of the assembly and function of glutamate receptor ion channels. Increasingly sophisticated biochemical, computational, and electrophysiological experiments are beginning to reveal the mechanism of action of partial agonists and suggest new models for the mechanism of action of allosteric modulators. Newly identified NMDA receptor ligands acting at novel sites offer hope for the development of subtype-selective modulators. The many unresolved issues include the role of the amino-terminal domain in AMPA receptor signaling and the mechanisms by which auxiliary proteins regulate receptor activity. The structural basis for ion permeation and ion channel block also remain areas of uncertainty, and despite substantial progress, molecular dynamics simulations have yet to reveal how glutamate binding opens the ion channel pore.
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