Fig. 1: Architecture of the CaV2.3-α2δ1−β1 complex.
From: Molecular insights into the gating mechanisms of voltage-gated calcium channel CaV2.3
a, b Cryo-EM map (a) and model (b) of the CaV2.3-α2δ1−β1 complex. The CaV2.3 α1E pore-forming subunit are colored pink, red, blue, and deep cyan. The C-terminal domain (CTD) of CaV2.3 are colored gray. The auxiliary subunits α2, δ, ανδ β1 are colored green, orange, and white, respectively. c The ion-conducting pathway and pore profiling of the CaV2.3. The ion-conducting pathway is viewed in parallel to the membrane and shown in black dots. The radius of the pore is calculated using the HOLE program. The vertical dashed line marks the 1.0-Å pore radius, which represents the ionic radius of calcium. d Superimposition of the DIII-IV fenestration between CaV2.3 and CaV1.1 complex. The nifedipine molecule bound to the CaV1.1 complex is shown as sticks. Residues stabilizing the nifedipine molecule in CaV1.1, and residues that might form steric clashes in CaV2.3 are shown as sticks. e Superimposition between the ‘P-loops’ (P1 and P2) and extracellular loops (ECLs) of the CaV2.3 and the ziconotide-bound CaV2.2. The CaV2.3 and CaV2.2 are shown as ribbon, overlaid with the ziconotide shown as transparent green surfaces. Potential steric clash between the ECLI of CaV2.3 and the ziconotide is highlighted in red. f Pathogenic mutations of the CaV2.3, shown in blue spheres. The four domains of CaV2.3 are colored pink, red, blue, and deep cyan, respectively. CaV1.1 is colored purple and CaV2.2 is colored gray.
