Supplementary Figure 3: Comparison with other helical-DD-fold structures.
From: Molecular basis of caspase-1 polymerization and its inhibition by a new capping mechanism
(a-c) Overall best alignment of the type I, II, and III dimers in caspase-1CARD filament (cyan, magenta, and green) with those in MAVSCARD filament (gray). (d) Structural alignment of caspase-1CARD and MAVSCARD as performed by the Dali server (Holm, L. & Sander, C.,Trends Biochem. Sci. 20, 478-480, 1995). Buried interfacial residues identified by PISA (Krissinel, E. & Henrick, K., J Mol Biol 372, 774-97, 2007) for each asymmetric dimer types were highlighted to show the similarity in their relative locations. (e) Comparison of relative angular differences in the caspase-1CARD filament (cyan, magenta, and green) and in the MAVSCARD filament, the PIDDosome complex, the Myddosome complex, and the ASCPYD filament. The left subunits (Ib, IIb, and IIIb monomers) are first aligned in the respective dimers, and the rotation angles required to bring the Ia, IIa, and IIIa monomers in superposition are indicated.
