Glutamate receptors at atomic resolution.
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.
Mayer
Mark L
ML
Building 35, Room 3B1002, Porter Neuroscience Research Center, 35 Lincoln Drive, Bethesda, Maryland 20892, USA. mayerm@mail.nih.gov
D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D018690:Excitatory Amino Acid Agonists / Q000378:metabolism / Q000494:pharmacology; D005544:Forecasting; D018698:Glutamic Acid / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008969:Molecular Sequence Data; D019636:Neurodegenerative Diseases / Q000378:metabolism; D018091:Receptors, AMPA / Q000737:chemistry / Q000378:metabolism; D017470:Receptors, Glutamate / Q000737:chemistry* / Q000378:metabolism
D018690:Excitatory Amino Acid Agonists; D007473:Ion Channels; D008024:Ligands; D018091:Receptors, AMPA; D017470:Receptors, Glutamate; D018698:Glutamic Acid