Abstract
Cloned NMDA receptor channels of the NR1-NR2A, NR1-NR2B and NR1-NR2C type show differences in argiotoxin636 block. Mutations of an asparagine residue located at a homologous position in the TM2 region of all NMDA receptor subunits, which corresponds to the Q/R site of the AMPA receptors, alters the argiotoxin636-induced block. The results suggest that the toxin interacts at this amino acid position with the putative pore forming TM2 region of the NMDA receptor subunits. Sequence differences in the TM2 segment of NR2A and NR2C subunits are not responsible for the subtype-specific sensitivity to argiotoxin636 as revealed by site-directed mutagenesis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Asparagine*
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Cloning, Molecular
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Female
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Glutamates / pharmacology
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Glutamic Acid
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Glutamine
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Glycine / pharmacology
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Indoleacetic Acids
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Kinetics
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Macromolecular Substances
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oocytes / drug effects
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Oocytes / physiology*
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Phenylacetates / pharmacology*
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Polyamines / pharmacology*
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Receptors, N-Methyl-D-Aspartate / antagonists & inhibitors*
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Receptors, N-Methyl-D-Aspartate / genetics
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Receptors, N-Methyl-D-Aspartate / physiology
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Recombinant Proteins / antagonists & inhibitors
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Recombinant Proteins / metabolism
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Spider Venoms / pharmacology*
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Xenopus laevis
Substances
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Glutamates
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Indoleacetic Acids
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Macromolecular Substances
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Phenylacetates
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Polyamines
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Receptors, N-Methyl-D-Aspartate
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Recombinant Proteins
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Spider Venoms
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Glutamine
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argiotoxin-636
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Glutamic Acid
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Asparagine
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Glycine