Abstract
Glutamate receptors mediate a vast array of processes in plants, animals and bacteria. In particular, the ionotropic glutamate receptors (iGluRs) are the most abundant excitatory neurotransmitter receptors in the mammalian central nervous system. Because these proteins are constructed from distinct folding domains, most of which can be traced to bacterial precursors, the analyses of these important receptor proteins has been performed on a variety of levels ranging from atomic structure and dynamics to behavioral studies. This review will focus on the structure and dynamics of iGluRs, with particular emphasis on the role that the glutamate-binding domain (S1S2) plays in receptor function.
Keywords: NR2 subunit, leucine binding protein, kainate receptors, Amino Terminal Domain, GluR2 S1S2
Current Drug Targets
Title: Structure of Glutamate Receptors
Volume: 8 Issue: 5
Author(s): Robert E. Oswald, Ahmed Ahmed, Michael K. Fenwick and Adrienne P. Loh
Affiliation:
Keywords: NR2 subunit, leucine binding protein, kainate receptors, Amino Terminal Domain, GluR2 S1S2
Abstract: Glutamate receptors mediate a vast array of processes in plants, animals and bacteria. In particular, the ionotropic glutamate receptors (iGluRs) are the most abundant excitatory neurotransmitter receptors in the mammalian central nervous system. Because these proteins are constructed from distinct folding domains, most of which can be traced to bacterial precursors, the analyses of these important receptor proteins has been performed on a variety of levels ranging from atomic structure and dynamics to behavioral studies. This review will focus on the structure and dynamics of iGluRs, with particular emphasis on the role that the glutamate-binding domain (S1S2) plays in receptor function.
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Cite this article as:
Oswald E. Robert, Ahmed Ahmed, Fenwick K. Michael and Loh P. Adrienne, Structure of Glutamate Receptors, Current Drug Targets 2007; 8 (5) . https://dx.doi.org/10.2174/138945007780618526
DOI https://dx.doi.org/10.2174/138945007780618526 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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