Extended Data Fig. 6: Structural details and sequence alignment of the pore domain and VSDs.
a, Overall structure of the pore domain of CATSPER1–4. The critical DDDD residues in the selectivity filter are shown as sticks. Each S6 segment contains a π-helix turn (red arrows). b, Sequence alignment of the selectivity filter and the pore helices among mouse CATSPER1–4, human CATSPER1–4, and rabbit Cav1.1. The invariant Thr and Trp residues are shaded cyan. The DDDD residues in the selectivity filter of CATSPER1–4 and the corresponding residues EEEE in Cav1.1 are highlighted red. c, Sequence alignment of the VSDs among CATSPER1–4. The boundary of each segment is shaded light grey. Positively charged residues on S4 segments are shaded blue and residues corresponding to positions R1–R6 are boxed. An1 and CTC residues on segments S2 and S3 are shaded purple. d, Structural comparison of the VSDs among CATSPER1–4. The four VSDs are superimposed relative to CTC and An1 on S2. For visual clarity, the S1 segments are omitted and only the side chains of aligned residues and R4 residues on the S4 segments are shown.
