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Amino acid residues in the transmembrane domain of the type 1 sigma receptor critical for ligand binding
Author(s) -
Yamamoto Hideko,
Miura Reiko,
Yamamoto Toshifumi,
Shinohara Keiko,
Watanabe Masayuki,
Okuyama Shigeru,
Nakazato Atsuro,
Nukada Toshihide
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00084-8
Subject(s) - transmembrane domain , sigma receptor , receptor , sigma , ligand (biochemistry) , amino acid , transmembrane protein , sigma 1 receptor , chemistry , biology , biochemistry , agonist , physics , quantum mechanics
The type 1 sigma receptor expressed in Xenopus oocytes showed binding abilities for the sigma‐1 ligands, [ 3 H](+)pentazocine and [ 3 H]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.