Fig. 3: Structure of the Needle/huNAIP/huNLRC4-R288A tripartite complex.
From: Structural basis of the human NAIP/NLRC4 inflammasome assembly and pathogen sensing
a, Cryo-EM map of Needle/huNAIP/huNLRC4-R288A Maps are colored by domain organization. b, Surface representation with highlighted interaction residues of huNAIP–huNLRC4 interfaces. The surface interfaces are colored to match their respective counterparts. The charged and ‘key’ residues are highlighted and colored on the basis of their properties: blue for positive, red for negative and yellow for hydrophobic. c, Magnified views of the interfaces with main and side chains in cartoon and sticks, respectively. d, Zoom-in views of huNAIP BIR domains. e, Magnified views of nucleotide-binding pockets in the open human NAIP (top) and NLRC4-R288A (bottom). Main and side chains of residues around ATP are shown as cartoon and sticks, respectively. f, Structure overlay of the open and modeled closed huNLRC4 at the nucleotide binding site. Wheat, ‘key’ from the catalytic open huNLRC4. The side chain of Phe435 and ADP is shown as sticks. Loop118–127 is highlighted.
