Population
L-type voltage-gated Ca2+ channels (pore-forming alpha1 subunit)
Comparison
Site-directed mutagenesis of amino acids within… vs Wild-type L-type calcium channels
Design
Preclinical
Authors
Loading...
Residue Y1048 and flanking sites in IIIS6/IVS6 are critical for dihydropyridine affinity; leaves open translation to native human channels or selective modulation.
Transmembrane segments IIIS6 and IVS6, specifically residue Tyr-1048, are critical for high-affinity dihydropyridine binding in L-type calcium channels.
Peterson et al. (1996) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: