IDENTIFICATION OF 1,4-DIHYDROPYRIDINE BINDING DOMAINS WITHIN THE PRIMARY STRUCTURE OF THE ALPHA-1 SUBUNIT OF THE SKELETAL-MUSCLE L-TYPE CALCIUM-CHANNEL
H. Kalasz et al., IDENTIFICATION OF 1,4-DIHYDROPYRIDINE BINDING DOMAINS WITHIN THE PRIMARY STRUCTURE OF THE ALPHA-1 SUBUNIT OF THE SKELETAL-MUSCLE L-TYPE CALCIUM-CHANNEL, FEBS letters, 331(1-2), 1993, pp. 177-181
Calcium channel blockers are drugs that bind to the alpha1 subunit of
L-type calcium channels and selectively inhibit ion movements through
these channels. Determination of the mechanism of channel blockade req
uires 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 label
ed receptor was purified and digested with trypsin. The labeled peptid
e fragments were immunoprecipitated with sequence-directed antibodies.
The data indicate the existence of at least three distinct dihydropyr
idine-binding domains within the primary structure of the alpha1 subun
it.