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Identification of 1,4‐dihydropyridine binding domains within the primary structure of the α 1 subunit of the skeletal muscle L‐type calcium channel
Author(s) -
Kalasz Huba,
Watanabe Toshiro,
Yabana Hideo,
Itagaki Kiyoshi,
Naito Kazuaki,
Nakayama Hitoshi,
Schwartz Arnold,
Vaghy Pal L.
Publication year - 1993
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(93)80321-k
Subject(s) - dihydropyridine , chemistry , protein subunit , calcium channel , protein primary structure , binding site , trypsin , n type calcium channel , l type calcium channel , biophysics , voltage dependent calcium channel , receptor , r type calcium channel , calcium , biochemistry , peptide sequence , biology , enzyme , t type calcium channel , organic chemistry , gene
Calcium channel blockers are drugs that bind to the α 1 subunit of L‐type calcium channels and selectively inhibit ion movements through these channels. Determination of the mechanism of channel blockade requires localization of drug‐binding sites within the primary structure of the receptor. In this study the 1,4‐dihydropyridine‐binding site of the membrane bound receptor has been identified. The covalently labeled receptor was purified and digested with trypsin. The labeled peptide fragments were immunoprecipitated with sequence‐directed antibodies. The data indicate the existence of at least three distinct dihydropyridine‐binding domains within the primary structure of the α 1 subunit.