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