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.
Publication types
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Research Support, N.I.H., Intramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Allosteric Regulation
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Amino Acid Sequence
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Animals
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Excitatory Amino Acid Agonists / metabolism
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Excitatory Amino Acid Agonists / pharmacology
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Forecasting
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Glutamic Acid / genetics
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Glutamic Acid / metabolism
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Humans
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Ion Channels / chemistry
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Ion Channels / metabolism
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Ligands
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Molecular Sequence Data
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Neurodegenerative Diseases / metabolism
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Receptors, AMPA / chemistry
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Receptors, AMPA / metabolism
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Receptors, Glutamate / chemistry*
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Receptors, Glutamate / metabolism
Substances
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Excitatory Amino Acid Agonists
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Ion Channels
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Ligands
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Receptors, AMPA
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Receptors, Glutamate
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Glutamic Acid