Site withinN-Methyl-d-aspartate Receptor Pore Modulates Channel Gating
نویسندگان
چکیده
منابع مشابه
Site within N-Methyl-D-aspartate receptor pore modulates channel gating.
N-methyl-d-aspartate-type glutamate receptors (NMDARs) are ligand-gated ion channels activated by coagonists glutamate and glycine. NMDARs play a critical role in synaptic plasticity and excitotoxicity, largely because of their high calcium permeability and slow deactivation and desensitization kinetics. NR1 is an obligate subunit in all NMDAR complexes, where it combines with NR2A, 2B, 2C, and...
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In this issue of Molecular Pharmacology, Low et al. (2003) delve into the mechanisms by which pH modulates the glutamate receptor subtype specifically activated by N–methylD-aspartate (NMDA). Based on a combination of scanning mutagenesis, patch clamp physiology, and molecular modeling, the authors conclude that amino acids involved in NMDA receptor modulation by protons are clustered in region...
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Background Anti-N-methyl- d-aspartate receptor (anti-NMDAR) encephalitis is an autoimmune neurological disorder that usually occurs as a paraneoplastic syndrome and is particularly associated with ovarian teratoma. Standard therapy for severe cases is not established and the prognosis in patients who do not respond to first-line treatment is poor. Case Report An 11-year-old boy complained ps...
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Extracellular protons inhibit N-methyl-D-aspartate (NMDA) receptors with an IC50 value in the physiological pH range. To identify the molecular determinants of proton sensitivity, we used scanning mutagenesis of the NR1 subunit to search for residues that control proton inhibition of NMDA receptors. Homology modeling of the extracellular domains suggested that residues at which mutations pertur...
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Ifenprodil is an allosteric inhibitor of GluN1/GluN2B N-methyl-D-aspartate receptors. Despite its widespread use as a prototype for drug development and a subtype-selective tool for physiologic experiments, its precise effect on GluN1/GluN2B gating is yet to be fully understood. Interestingly, recent crystallographic evidence identified that ifenprodil, unlike zinc, binds at the interface of th...
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ژورنال
عنوان ژورنال: Molecular Pharmacology
سال: 2004
ISSN: 0026-895X,1521-0111
DOI: 10.1124/mol.65.1.157