Fig. 5: Structure basis for blockade of CaV3.3 by pimozide.
From: Structure, gating, and pharmacology of human CaV3.3 channel
a Chemical structures of pimozide. b The cryo-EM density shown in blue mesh for PMZ in sticks. c Cross-sectional view, showing the open selectivity filter, fenestrations, pore domain where PMZ (blue spheres) located and intracellular gate. Phospholipids entering through other fenestrations are displayed as white sticks. d Detailed binding sites for pimozide. The side chains of key residues are displayed in sticks and the hydrophobic side chains are overlaid with transparent surfaces. Black dashed lines indicated potential hydrogen bonds. e Comparison of CaV3.3PMZ with CaV3.3apo (wheat). The shifts of the backbone of S6III helix and side chain of L1423 and F1426 and phosphate group of the phospholipid are indicated by red arrows.
