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. 2020 Jun 24;472(7):755–773. doi: 10.1007/s00424-020-02418-w

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© The Author(s) 2020

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Fig. 3 — CACNA1D structural models. (A) A homology model of the inactivated state based on rabbit Cav1.1 (PDB entry 5gjv, [93]). Transmembrane segments of homologous repeats I (cyan) and II (blue) are shown with germline de novo missense variants highlighted as orange sticks. They spatially cluster around the activation gate formed by S6-helices of repeats I and II. (B) The homology model of the CACNA1D resting state (based on PDB entry 6p6w, [92]) shows that A749 and G403 (orange spheres) tightly interact with surrounding residues on the S5 helix and S4-S5 linker (highlighted as spheres). Cartoon and carbon atoms depicted as spheres are colored according to the homologous repeats, whereas nitrogen and oxygen atoms of residues depicted as spheres are colored blue and red, respectively. (C) The pore-forming helix S6 requires conformational rearrangements of the backbone to facilitate pore opening in the activated state (green cartoon) compared with the resting state (cyan cartoon). G407 (S6 in repeat I) is highlighted in orange (resting state) and yellow (activated state)