2007
DOI: 10.1590/s0100-879x2007001100001
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Abstract: Ionotropic glutamate receptors are major excitatory receptors in the central nervous system and also have a far reaching influence in other areas of the body. Their modular nature has allowed for the isolation of the ligand-binding domain and for subsequent structural studies using a variety of spectroscopic techniques. This review will discuss the role of specific ligand:protein interactions in mediating activation in the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype of glutamate receptors as e… Show more

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Cited by 5 publications
(4 citation statements)
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“…However, most of the structures are of the ␣-amino-5-methyl-3-hydroxy-4-isoxazole propionate (AMPA) subtype, for which currently there are Ͼ60 structures in various ligated states (1,8,11). There is also significant insight into the dynamic state of the agonist binding domain for the AMPA receptors and on the role of specific agonist-protein interactions (9,(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26). These studies show that for a number of cases the agonist binding domains (ABDs) 3 of the AMPA receptors show a graded cleft closure with the extent of cleft closure correlating to the extent of activation (efficacy) of the agonist.…”
mentioning
confidence: 99%
“…However, most of the structures are of the ␣-amino-5-methyl-3-hydroxy-4-isoxazole propionate (AMPA) subtype, for which currently there are Ͼ60 structures in various ligated states (1,8,11). There is also significant insight into the dynamic state of the agonist binding domain for the AMPA receptors and on the role of specific agonist-protein interactions (9,(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26). These studies show that for a number of cases the agonist binding domains (ABDs) 3 of the AMPA receptors show a graded cleft closure with the extent of cleft closure correlating to the extent of activation (efficacy) of the agonist.…”
mentioning
confidence: 99%
“…Recent vibrational spectroscopic investigations ( ) in combination with fluorescence resonance energy transfer (FRET) studies ( 5 , 8 , 9 ) on the isolated ligand binding domain of the GluR2 subunit (GluR2-S1S2) have provided insight into the role of specific ligand−protein interactions in mediating AMPA receptor activation. By using these techniques to study activation by the three ligands kainate, AMPA, and glutamate on wild type and mutant proteins, which provide a wide spectrum of activations, a correlation was developed between the changes at specific ligand−protein interactions and the extent of activation of the channel.…”
mentioning
confidence: 99%
“…Significant insight into the mechanism by which the agonist mediates receptor activation has been obtained by the large number of structural investigations on the isolated extracellular ligand binding domain , . These structural investigations, in combination with the vast existing electrophysiological data on the native receptor , suggest that the cleft closure conformational change induced by agonist binding is one of the key coupling mechanisms between the ligand binding domain and the channel segments ,, . While the structures of this isolated domain have provided invaluable insight into the allosteric mechanism, they are limited by the fact that the domain is isolated and in the absence of the functional ion channel segments.…”
mentioning
confidence: 99%
“…Most fast excitatory signaling in the mammalian brain is mediated by ionotropic AMPA-type glutamate receptors, with glutamate binding to an extracellular domain on the postsynaptic AMPA 1 receptors leading to the opening of a cationselective channel that results in depolarization of the receiving cell (1)(2)(3)(4)(5). Significant insight into the mechanism by which the agonist mediates receptor activation has been obtained by the large number of structural investigations on the isolated extracellular ligand binding domain (3,(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22). These structural investigations, in combination with the vast existing electrophysiological data on the native receptor (23)(24)(25), suggest that the cleft closure conformational change induced by agonist binding is one of the key coupling mechanisms between the ligand binding domain and the channel segments (3,16,20).…”
mentioning
confidence: 99%