Review Article | Published:

Glutamate receptors at atomic resolution

Nature volume 440, pages 456462 (23 March 2006) | Download Citation

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Abstract

At synapses throughout the brain and spinal cord, the amino-acid glutamate is the major excitatory neurotransmitter. During evolution, a family of glutamate-receptor ion channels seems to have been assembled from a kit consisting of discrete ligand-binding, ion-channel, modulatory and cytoplasmic domains. Crystallographic studies that exploit this unique architecture have greatly aided structural analysis of the ligand-binding core, but the results also pose a formidable challenge, namely that of resolving the allosteric mechanisms by which individual domains communicate and function in an intact receptor.

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Acknowledgements

Work in the author's laboratory is supported by the intramural research programme of NICHD, NIH, DHHS. Synchotron diffraction data were collected at Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory. Use of the Advanced Photon Source was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences.

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  1. Building 35, Room 3B1002, Porter Neuroscience Research Center, 35 Lincoln Drive, Bethesda, Maryland 20892, USA. mayerm@mail.nih.gov

    • Mark L. Mayer

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The author declares no competing financial interests.

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https://doi.org/10.1038/nature04709

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