Glutamate receptors at atomic resolution
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.
- Authors:
-
- NIH
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1007698
- Resource Type:
- Journal Article
- Journal Name:
- Nature
- Additional Journal Information:
- Journal Volume: 440; Journal Issue: 03, 2006
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; ARCHITECTURE; BRAIN; RESOLUTION; SPINAL CORD
Citation Formats
Mayer, Mark L. Glutamate receptors at atomic resolution. United States: N. p., 2010.
Web. doi:10.1038/nature04709.
Mayer, Mark L. Glutamate receptors at atomic resolution. United States. https://doi.org/10.1038/nature04709
Mayer, Mark L. 2010.
"Glutamate receptors at atomic resolution". United States. https://doi.org/10.1038/nature04709.
@article{osti_1007698,
title = {Glutamate receptors at atomic resolution},
author = {Mayer, Mark L},
abstractNote = {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.},
doi = {10.1038/nature04709},
url = {https://www.osti.gov/biblio/1007698},
journal = {Nature},
number = 03, 2006,
volume = 440,
place = {United States},
year = {Fri Dec 03 00:00:00 EST 2010},
month = {Fri Dec 03 00:00:00 EST 2010}
}
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