Extended Data Fig. 9: Multiple sequence alignment of NLRP3 proteins.
From: Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3
Secondary structure elements are indicated for human NLRP3 as determined here. Subdomain boundaries are labelled and conserved sequence motifs are written italic. Residues in the decamer assembly interfaces A, B and C are labelled with asterisks. Smaller asterisks correspond to 10–50, larger to > 50 Å2 buried surface area, respectively. Pathogenic disease mutations FCAS1 (familial cold auto-inflammatory syndrome 1), CINCA (chronic infantile neurological cutaneous articular), MWS (Muckle-Wells syndrome) and CAPS (Cryopyrin associated periodic syndrome) are marked with circles as indicated. Sequences of human (UniProt accession number Q96P20), macaque (B0FPE9), mouse (Q8R4B8), rat (D4A523), and bovine (A6QLE5) NLRP3 proteins were aligned with MultAlin and the secondary structure annotated with ESPript50.
