Ligand--protein interactions in the glutamate receptor.
Fourier transform infrared spectroscopy was used to investigate ligand-protein interactions in the ligand-binding domain of the GluR4 glutamate receptor subunit. Glutamate binding induces more extensive secondary structural changes in the ligand-binding domain than does kainate binding. Glutamate also alters the hydrogen bonding strength of the single free cysteine side chain in the domain, while kainate does not. On the other hand, the interaction of a binding site arginine residue with kainate appears to be stronger than that with glutamate. These results identify chemical and structural differences that may explain the different functional characteristics of the two agonists acting on ionotropic glutamate receptors. In doing so, they complement and extend recent crystallographic structures of the ligand-binding domain.
Chemistry Department, Marquette University, Milwaukee, Wisconsin 53233, USA. vasanthi.jayaraman@marquette.edu
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D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D018698:Glutamic Acid / Q000737:chemistry / Q000378:metabolism*; D007608:Kainic Acid / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D018091:Receptors, AMPA / Q000737:chemistry* / Q000378:metabolism*; D012996:Solutions; D017550:Spectroscopy, Fourier Transform Infrared
D008024:Ligands; D018091:Receptors, AMPA; D012996:Solutions; C104724:glutamate receptor ionotropic, AMPA 4; D018698:Glutamic Acid; D003545:Cysteine; D007608:Kainic Acid