Structural Features of the Glutamate Binding Site in Recombinant NR1/NR2A N-Methyl-d-aspartate Receptors Determined by Site-Directed Mutagenesis and Molecular Modeling

@article{Chen2005StructuralFO,
  title={Structural Features of the Glutamate Binding Site in Recombinant NR1/NR2A N-Methyl-d-aspartate Receptors Determined by Site-Directed Mutagenesis and Molecular Modeling},
  author={Philip E. Chen and Matthew T. Geballe and Phillip J. Stansfeld and Alexander R. Johnston and Hongjie Yuan and Amanda L Jacob and James P. Snyder and Stephen F. Traynelis and David J A Wyllie},
  journal={Molecular Pharmacology},
  year={2005},
  volume={67},
  pages={1470 - 1484}
}
  • Philip E. Chen, Matthew T. Geballe, +6 authors David J A Wyllie
  • Published 2005
  • Medicine, Biology
  • Molecular Pharmacology
  • We have used site-directed mutagenesis of amino acids located within the S1 and S2 ligand binding domains of the NR2A N-methyl-d-aspartate (NMDA) receptor subunit to explore the nature of ligand binding. Wild-type or mutated NR1/NR2A NMDA receptors were expressed in Xenopus laevis oocytes and studied using two electrode voltage clamp. We investigated the effects of mutations in the S1 and S2 regions on the potencies of the agonists l-glutamate, l-aspartate, (R,S)-tetrazol-5yl-glycine, and NMDA… CONTINUE READING

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