Analysis of the glycine binding domain of the NMDA receptor channel zeta 1 subunit.
In an attempt to examine glycine binding domain of the zeta 1 subunit of the mouse N-methyl-D-aspartate (NMDA) receptor channel, we constructed N-terminal or C-terminal deletion mutants of the zeta 1 subunit cDNA and expressed them in Spodoptera frugiperda cells using a baculovirus system. Analysis of binding of a glycine binding site antagonist, 5,7-[3(-3)H]dichlorokynurenate ([3H]DCKA) to the deleted zeta 1 mutants provided the first direct experimental evidence that the regions of N-terminal 282 and C-terminal 102 amino acid residues do not significantly affect glycine binding, and that both the region of approximately 260 amino acid residues preceding the putative transmembrane segment M1 and the region between the segments M3 and M4 are required to form the glycine binding domain.
Uchino
S
S
Molecular Medicine Laboratory, Yokohama Research Center, Mitsubishi Chemical Corporation, Yokohama, Japan.
Nakajima-Iijima
S
S
Okuda
K
K
Mishina
M
M
Kawamoto
S
S
D000818:Animals; D002462:Cell Membrane / Q000187:drug effects*; D002478:Cells, Cultured; D005998:Glycine / Q000494:pharmacology*; D051379:Mice; D011869:Radioligand Assay; D016194:Receptors, N-Methyl-D-Aspartate / Q000032:analysis* / Q000187:drug effects*
D016194:Receptors, N-Methyl-D-Aspartate; D005998:Glycine