Allosteric interaction between zinc and glutamate binding domains on NR2A causes desensitization of NMDA receptors

Fast desensitization is an important regulatory mechanism of neuronal NMDA receptor function. Previous work suggests that fast desensitization of NR1/NR2A receptors is caused by ambient zinc, and that a positive allosteric interaction occurs between the extracellular zinc-binding amino terminal doma...

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Veröffentlicht in:	The Journal of physiology 2005-12, Vol.569 (2), p.381-393
Hauptverfasser:	Erreger, Kevin, Traynelis, Stephen F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation - physiology Binding Sites Cell Line Data Interpretation, Statistical Excitatory Postsynaptic Potentials - drug effects Excitatory Postsynaptic Potentials - physiology Glutamic Acid - metabolism Glutamic Acid - pharmacology Glycine - metabolism Glycine - pharmacology Humans Hydrogen-Ion Concentration Membrane Potentials - drug effects Membrane Potentials - physiology Models, Biological Molecular and Genomic Physiology Patch-Clamp Techniques Protein Binding Receptors, N-Methyl-D-Aspartate - chemistry Receptors, N-Methyl-D-Aspartate - drug effects Receptors, N-Methyl-D-Aspartate - physiology Time Factors Zinc - metabolism Zinc - pharmacology
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