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Kinetic model used to model binding and unbinding of glutamate and D-AA

Ensemble averages currents following 2ms pulses of glutamate in Ringer and in the competitive antagonist D-AA. Kinetic model used to model binding and unbinding of glutamate and D-AA. NMDA receptor open time depends on high affinity and slow agonist unbinding.

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Kinetic model used to model binding and unbinding of glutamate and D-AA

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  1. Ensemble averages currents following 2ms pulses of glutamate in Ringer and in the competitive antagonist D-AA

  2. Kinetic model used to model binding and unbinding of glutamate and D-AA

  3. NMDA receptor open time depends on high affinity and slow agonist unbinding

  4. 5-HT1B receptors reduce peak cleft glutamate concentrations in CA1- subicular synapses

  5. By lowering synaptic cleft glutamate concentrations, presynaptic 5-HT1B receptors can differentially modulate postsynaptic receptors with different sensitivities to glutamate

  6. Modular organization of a glutamate receptor Mayer (2006) Nature440, 456-462

  7. Activation of iGluR gating, resulting from agonist-induced expansion of the ligand-binding core dimer

  8. Conserved structural elements in the agonist-binding site of iGluRs

  9. The L483Y mutation and CTZ promote dimerization and block desensitization Yu Sun et al (2002) Nature 417, 245-253

  10. Agonist-induced conformational changes in the dimer and gating model

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