Báo cáo Y học: Determinants of antagonist binding at the a-amino-3-hydroxy5-methyl-4-isoxazolepropionic acid receptor subunit, GluR-D Role of the conserved arginine 507 and glutamate 727 residues
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Previous structural andmutagenesis studies indicate that the invariant a-amino and a-carboxyl groups of glutamate receptor agonists are engaged in polar interactions with oppositely charged, conserved arginine and glutamate resi-dues in the ligand-binding domain ofa-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor.To examine the role of these residues (R507 and E727 in the GluR-D subunit) in the discrimination between agonists and anta-gonists, we analyzed the ligand-binding properties of homomeric GluR-D and its soluble ligand-binding domain withmutations at thesepositions....
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