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Identification of 1,4-dihydropyridine binding domains within the primary structure of the α1subunit of the skeletal muscle L-type calcium channel

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
331
Identifiers
DOI: 10.1016/0014-5793(93)80321-k
Keywords
  • Calcium Channel Blocker
  • 1
  • 4-Dihydropyridine Receptor

Abstract

Abstract 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.

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