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Identification of a domain of ET A receptor required for ligand binding
Author(s) -
Adachi Miki,
Yang Yan-Yan,
Trzeciak Arnold,
Furuichi Yasuhiro,
Miyamoto Chikara
Publication year - 1992
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 - 10.1016/0014-5793(92)81393-z
Subject(s) - receptor , extracellular , chemistry , ligand (biochemistry) , enzyme linked receptor , domain (mathematical analysis) , loop (graph theory) , 5 ht5a receptor , protease activated receptor 2 , biophysics , biology , biochemistry , mathematics , mathematical analysis , combinatorics
Various chimeric ET A and ET B receptors were produced in CHO cells for the elucidation of a specific domain which influences the affinity of the receptor toward BQ‐123, a selective ET A antagonist. Replacement of the first extracellular loop domain (B‐loop) of the ET A receptor with the corresponding domain of the ET B receptor, reduced the inhibition by BQ‐123 drastically, while the replacements of other extracellular domains of ET A did not. By contrast, the introduction of the B‐loop of ET A in place of the corresponding domain of the ET B receptor endowed the ET B ‐based chimeric receptor with a sensitivity to BQ‐123. These observations suggest that the B‐loop domain of the ET A receptor is involved in ligand binding.