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Review
. 2007 Nov;40(11):1419-27.
doi: 10.1590/s0100-879x2007001100001.

Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships

K A Mankiewicz  1 , V Jayaraman
Affiliations
Review

Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships

K A Mankiewicz et al. Braz J Med Biol Res. 2007 Nov.

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 a-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype of glutamate receptors as established by various spectroscopic investigations of the GluR2 and GluR4 subunits of this receptor. Specifically, this review will provide an introduction to the insight gained from X-ray crystallography and nuclear magnetic resonance investigations and then go on to focus on studies utilizing vibrational spectroscopy and fluorescence resonance energy transfer to study the behavior of the isolated ligand-binding domain in solution and discuss the importance of specific ligand:protein interactions in the mechanism of receptor activation.

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Figures

Figure 1
Figure 1
Crystal structure of GluR2-S1S2 protein with glutamate bound (19). Sites that were tagged with fluorescent labels for FRET measurements are highlighted.
Figure 2
Figure 2
The environment of the ligand glutamate in GluR2-S1S2 (19). The side chain residues interacting with the ligand are shown.
Figure 3
Figure 3
Distance between N-terminus/residue 394 and residue S652 as determined by FRET for the GluR2-S1S2 wild type and L650T and Y450F mutants plotted as a function of extent of activation for the apo and AMPA-, glutamate-, and kainate-bound states (37). Reproduced with permission from Biochemistry 2007; 46: 1343–1349. Copyright 2007 American Chemical Society.
Figure 4
Figure 4
Schematic representation of the structural changes associated with the two-phase ligand binding process for the GluR2-S1S2 domain binding to glutamate (32). Reproduced with permission from Nat. Chem. Biol. 2005;1: 329–332. Copyright 2005 Nature Publishing Group.
See this image and copyright information in PMC

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