Fig. 1: Architecture of the CaV1.2 complex.
From: Structural bases of inhibitory mechanism of CaV1.2 channel inhibitors
a, b The overall EM density map and structure of the CaV1.2 complex. The α2δ1 and β2b subunits, voltage-sensing domain (VSD), C-terminal domain (CTD), α-interacting domain (AID), and N-glycans were labeled. The α1 subunit is colored in deep green (Domain I, DI: A114-R211, F231-I447), light green (DII: W509-K778), deep blue (DIII: F889-I943, F964-Y1197), mauve (DIV: K1198-S1321, E1350-T1357, S1372-E1484, P1494-D1533), and orange (CTD: W1534-P1574, C1582-S1593, N1607-K1638, K1647-P1655), respectively. The β2b (D222-R276, L297-W407), α2 (F27-D129, Q143-V224, K232-N540, Q554-K690, N698-T828, D849-P906), and δ1 (Q972-G1022, T1028-D1070) subunits are colored in magenta, turquoise, and pink, respectively. N-glycans are colored in yellow. c The ion permeation path in the pore domain. The selectivity filter and S5-S6 helices are shown in cartoon and viewed in parallel to the membrane plane. The ion conducting pathway was calculated by using the program HOLE and illustrated with gray dots. d Plot of pore radii for the CaV1.2 complex. e The selectivity filter ring of four glutamate residues from the four domains of CaV channel were shown in sticks. A cation ion is shown as a green sphere. f The intracellular gate formed by four S6 helices viewed from the intracellular side. Hydrophobic residues are shown in sticks.
