| Literature DB >> 16554805 |
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.Entities:
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Year: 2006 PMID: 16554805 DOI: 10.1038/nature04709
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962