期刊论文详细信息
FEBS Letters
Amino acid residues in the transmembrane domain of the type 1 sigma receptor critical for ligand binding
Yamamoto, Toshifumi1  Nakazato, Atsuro3  Nukada, Toshihide2  Miura, Reiko2  Watanabe, Masayuki1  Okuyama, Shigeru3  Shinohara, Keiko1  Yamamoto, Hideko1 
[1] Department of Psychopharmacology, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-8585, Japan;Department of Neurochemistry, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-8585, Japan;The 1st Laboratory, Medicinal Research Laboratory, Taisho Pharmaceutical, Saitama 330-8530, Japan
关键词: Type 1 sigma receptor;    Xenopus oocyte;    Ligand binding;    Immunoblot analysis;    Site-directed mutagenesis;    Transmembrane domain;    SigmaR1;    type 1 sigma receptor;    NE-100;    N;    N-dipropyl-2-(4-methoxy-3-(2-phenylethoxy)phenyl)-ethylamine monohydrochloride;    PCR;    polymerase chain reactions;    HRP;    horseradish peroxidase;    K d;    dissociation constant;   
DOI  :  10.1016/S0014-5793(99)00084-8
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The type 1 sigma receptor expressed in Xenopus oocytes showed binding abilities for the sigma-1 ligands, [3H](+)pentazocine and [3H]NE-100, with similar kinetic properties as observed in native tissue membranes. Amino acid substitutions (Ser99Ala, Tyr103Phe and di-Leu105,106di-Ala) in the transmembrane domain did not alter the expression levels of the type 1 sigma receptor as determined by immunoblot analysis using an anti-type 1 sigma receptor antiserum. By contrast, ligand binding was significantly suppressed by the substitutions. These findings provide evidence that the transmembrane domain of the type 1 sigma receptor plays a critical role in ligand binding of this receptor.

【 授权许可】

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