Figure 3
(A) Linear topology schematic of pore forming CaVα1 subunits. Domains I–IV contain six homologous transmembrane segments where the S1–S4 segments form a voltage-sensor paddle with multiple positively charged amino acids (+) found in S4. S5–56 form the pore with the pore loop (P) folding back into the membrane to form the selectivity filter. (B) Schematic of a VGCC complex with a CaVα1 bound to its CaVβ and CaVα2-δ subunits (GPI, glycosylphosphatidylinositol anchor). Domain IV and the C-terminal tail have been removed. (C) Evolutionary tree of CaVα1subunits.
VGCCs are composed of a pore-forming subunit and associated accessory subunits

(A) Linear topology schematic of pore forming CaVα1 subunits. Domains I–IV contain six homologous transmembrane segments where the S1–S4 segments form a voltage-sensor paddle with multiple positively charged amino acids (+) found in S4. S5–56 form the pore with the pore loop (P) folding back into the membrane to form the selectivity filter. (B) Schematic of a VGCC complex with a CaVα1 bound to its CaVβ and CaVα2-δ subunits (GPI, glycosylphosphatidylinositol anchor). Domain IV and the C-terminal tail have been removed. (C) Evolutionary tree of CaVα1subunits.

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