Fig. 3: Structural dynamics of ARD and CCD of TRPC1/C4/C5 channels in lipid nanodiscs.
From: Molecular architecture of the human TRPC1/C5 heteromeric channel
a Ankyrin repeat domain (ARD) and coiled-coil domain (CCD) conformation of the TRPC5 homomer from the TRPC1/C5 heteromer dataset (left). Class 1 shows more extended arrangement, whereas Class 2 exhibits a clockwise ARD rotation and CCD tilt, resulting in reduced ARD–CCD distance with the adjacent subunit. b In the TRPC1/C4 heteromer (PDB: 8WPL), the CCD adopts a straight conformation. All subunits (one TRPC1 and three TRPC4 subunits) show close ARD–CCD proximity. c In the TRPC1/C5 heteromer, the ARD–CCD axis is non-linear, with the CCD tilted toward the TRPC1 and TRPC5D subunits. Alignment across chains reveals varied ARD–CCD distances, highlighted in angstroms (Å).
