Fig. 2: Cryo-EM structure of full-length Caspase-1.
From: Atomic mechanisms of full-length ASC-mediated inflammasome assembly
a Helical reconstruction of full-length Caspase-1CARD filament overlaid with atomic models shown in different colors; one CARD subunit (green, in the red dashed box) is zoomed in. b Superposition of full-length Caspase-1CARD subunit (green) with Caspase-1CARD-alone (PDB accession code: 5FNA, in grey), where the Cα traces of α1 and α1A helices have different registers (in the red dashed ellipsoid). c Zoom-in of the Cα traces of α1 and α1A helices (in the red dashed ellipsoid) and electron density for full-length Caspase-1CARD to support its atomic structure. d Location of trimeric interactions in full-length Caspase-1CARD filament; the trimeric interface highlighted in red solid circle is zoomed in with the closest inter-residue interactions labeled. e Superposition of full-length Caspase-1CARD (shown in color) and full-length ASCCARD (grey) filaments in the trimeric region to show the compatibility of the interfaces.
