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J Biol Chem, Vol. 273, Issue 32, 19933-19937, August 7, 1998
From the Glycine is an essential co-agonist of the
excitatory N-methyl-D-aspartate (NMDA)
receptor, a subtype of the ionotropic glutamate receptor family. The
glycine binding site of this hetero-oligomeric ion channel protein is
formed by two distinct extracellular regions, S1 and S2, of the NR1
subunit, whereas the homologous domains of the NR2 subunit mediate
glutamate binding. Here, segments S1 and S2 of the NR1 polypeptide were
fused via a linker peptide followed by N- and C-terminally
tagging with Flag and His6 epitopes, respectively.
Infection of High Five insect cells with a recombinant baculovirus
containing this glycine binding site construct resulted in efficient
secretion of a soluble fusion protein of about 53 kDa. After affinity
purification to near-homogeneity, the fusion protein bound the
competitive glycine site antagonist [3H]MDL105,519 with
high affinity (Kd = 5.22 ± 0.13 nM) similar to that determined with rat brain membrane
fractions. This high affinity binding could be competed by the glycine
site antagonist 7-chlorokynurenic acid as well as the agonists glycine and D-serine but not by L-glutamate. This
indicates that the S1 and S2 domains of the NR1 subunit are sufficient
for the formation of a glycine binding site that displays
pharmacological properties similar to those of the NMDA receptor
in vivo.
Expression and Initial Characterization of a Soluble Glycine
Binding Domain of the N-Methyl-D-aspartate
Receptor NR1 Subunit
,, and
Department of Neurochemistry,
e 46 and
the § Department of Molecular Membrane Biology,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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