[HTML][HTML] Mechanism of dihydropyridine interaction with critical binding residues of L-type Ca2+ channel α1 subunits
E Wappl, J Mitterdorfer, H Glossmann… - Journal of Biological …, 2001 - ASBMB
We investigated the mechanism of interaction of individual L-type channel amino acid
residues with dihydropyridines within a dihydropyridine-sensitive α1A subunit (α1A DHP).
Mutation of individual residues in repeat III and expression in Xenopus oocytes revealed that
Thr 1393 is not required for dihydropyridine interaction but that bulky side chains (tyrosine,
phenylalanine) in this position sterically inhibit dihydropyridine coordination. In position
1397 a side chain carbonyl group was required for high antagonist sensitivity. Agonist …
residues with dihydropyridines within a dihydropyridine-sensitive α1A subunit (α1A DHP).
Mutation of individual residues in repeat III and expression in Xenopus oocytes revealed that
Thr 1393 is not required for dihydropyridine interaction but that bulky side chains (tyrosine,
phenylalanine) in this position sterically inhibit dihydropyridine coordination. In position
1397 a side chain carbonyl group was required for high antagonist sensitivity. Agonist …