GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists
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X-ray structures of the GluR2 ligand-binding core in complex with (S)-Des-Me-AMPA and in the presence and absence of zinc ions have been determined. (S)-Des-Me-AMPA, which is devoid of a substituent in the 5-position of the isoxazolol ring, only has limited interactions with the partly hydrophobic pocket of the ligand-binding site, and adopts an AMPA-like binding mode. The structures, in comparison with other agonist complex structures, disclose the relative importance of the isoxazolol ring and of the substituent in the 5-position for the mode of binding. A relationship appears to exist between the extent of interaction of the ligand with the hydrophobic pocket and the affinity of the ligand.
Original language | English |
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Journal | F E B S Letters |
Volume | 531 |
Issue number | 2 |
Pages (from-to) | 173-8 |
Number of pages | 6 |
ISSN | 0014-5793 |
Publication status | Published - 6 Nov 2002 |
- Animals, Binding Sites, Crystallography, X-Ray, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Isoxazoles, Ligands, Macromolecular Substances, Methionine, Models, Molecular, Peptides, Protein Binding, Receptors, AMPA, Sulfates, Zinc, alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
Research areas
ID: 44729582