Extended Data Fig. 1: Brief introduction to Cav channels.
From: Cryo-EM structures of apo and antagonist-bound human Cav3.1
a, A brief overview of the classification, physiology and pharmacology of mammalian Cav channels. The evolutionary distance is calculated by Clustal W55. The table is summarized from several reviews4,20,56,57. HVA, high-voltage-activated; LVA, low-voltage-activated; E-C coupling, excitation–contraction coupling; E-T coupling, excitation–transcription coupling. b, Pairwise comparison of sequence similarity and identity of full-length human Cav channels. The sequence alignment is provided as Supplementary Fig. 1. c, Topological structure of the Cav channels. The panel is adapted from our previous publication with some modifications23. For Cav3.1-Δ8b, residues 509–642, shown as dashed lines on the I–II linker, were deleted. No human splice variant corresponding to the mouse Cav3.1-Δ8b has been identified. In fact, the exon–intron boundaries do not support existence of such a variant in humans. Nevertheless, we name this construct Cav3.1-Δ8b to acknowledge the source where this construct was generated. Five glycosylation sites are observed on the extracellular loops, including Asn246/322/1428/1425/1675 (Fig. 1a). Glycosylation of the counterparts of Asn246 and Asn1425 has been reported in Cav3.258,59, and the glycosylation might modulate channel expression and activity60,61,62. d, The typical domain-swapped architecture of most voltage-gated ion channels63. Shown here is an extracellular view in which the voltage-sensing domains are shown as round rectangles.
