Extended Data Fig. 3: The 3-Helix configuration of the new calsequestrin filament candidate promotes close packing of thioredoxin domains.
From: The structure of a calsequestrin filament reveals mechanisms of familial arrhythmia
a, The candidate cardiac calsequestrin filament assembled from crystallographic symmetry operations on PDB ID 6OWV (human CASQ2, this study). The filament exhibits tight packing of protomers and thioredoxin domains (shown on the right using equal-size spheres placed at the center of mass of each thioredoxin domain). b, A putative skeletal calsequestrin filament assembled from crystallographic symmetry operations on PDB ID 1A8Y (rabbit CASQ1, 1998). Right-side: equal-size spheres represent thioredoxin domains. c, A putative skeletal calsequestrin filament assembled from crystallographic symmetry operations on PDB ID 1SJI (canine CASQ2, 2005). Right-side: equal-size spheres represent thioredoxin domains.
