Uchino S, Nakajima-Iijima S, Okuda K, Mishina M, Kawamoto S
Molecular Medicine Laboratory, Yokohama Research Center, Mitsubishi Chemical Corporation, Yokohama, Japan.
Neuroreport. 1997 Jan 20;8(2):445-9. doi: 10.1097/00001756-199701200-00014.
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.
为了研究小鼠N-甲基-D-天冬氨酸（NMDA）受体通道ζ1亚基的甘氨酸结合结构域，我们构建了ζ1亚基cDNA的N端或C端缺失突变体，并使用杆状病毒系统在草地贪夜蛾细胞中进行表达。分析甘氨酸结合位点拮抗剂5,7-[3(-3)H]二氯犬尿氨酸（[3H]DCKA）与缺失的ζ1突变体的结合情况，首次提供了直接实验证据，表明N端282个氨基酸残基区域和C端102个氨基酸残基区域对甘氨酸结合没有显著影响，并且在假定的跨膜片段M1之前约260个氨基酸残基的区域以及片段M3和M4之间的区域都是形成甘氨酸结合结构域所必需的。
