The structure and function of glutamate receptor ion channels
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Neuroscience
Link
http://www.nature.com/articles/nrn725.pdf
Reference146 articles.
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2. Sakmann, B. & Neher, E. (eds) Single Channel Recording (Plenum, New York, 1983).
3. Armstrong, N., Sun, Y., Chen, G.-Q. & Gouaux, E. Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913–917 (1998). The first atomic-resolution structure of a glutamate receptor ligand-binding domain.
4. Armstrong, N. A. & Gouaux, E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28, 165–181 (2000). Crystallographic structures of the iGluR ligand-binding domain in the apo state and in a complex with agonists and antagonists revealed cleft closure on agonist binding. The extent of closure correlates with the extent of channel activation by a given agonist, providing the first model of iGluR activation.
5. Mayer, M. L., Olson, R. & Gouaux, E. Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state. J. Mol. Biol. 311, 815–836 (2001). This study provides the first evidence of dimerization of the ligand-binding domain in solution. The crystallographic structure of the ligand-free prokaryotic iGluR ligand-binding domain revealed a closed cleft, indicating an open–closed equilibrium that is probably reflected in spontaneous activity of the channel.
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