THE L-type voltage-dependent calcium channel is an important link in excitation-contraction coupling of muscle cells¹ (reviewed in refs 2 and 3). The channel has two functional characteristics: calcium permeation and receptor sites for calcium antagonists. In skeletal muscle the channel is a complex of five subunits, α₁, α₂, β, γ and δ (ref. 4). Complementary DNAs to these subunits have been cloned and their amino-acid sequences deduced^5–8. The skeletal muscle α₁ subunit cDNA expressed in L cells manifests as specific calcium-ion permeation, as well as sensitivity to the three classes of organic calcium-channel blockers^9,10. We report here that coexpression of the α₁, subunit with other subunits results in significant changes in dihydropyridine binding and gating properties. The available number of drug receptor sites increases 10-fold with an α₁ β combination, whereas the affinity of the dihydropyridine binding site remains unchanged. Also, the presence of the β subunit accelerates activation and inactivation kinetics of the calcium-channel current.