Domain organization, ATP-binding motifs and structural overview of NLRP^NACHT 3D models.

(A) NLRPs show tripartite domain architecture (PYD-NACHT-LRR) except NLRP1 (which possesses two additional C-terminal domains: FIIND and CARD) and NLRP10 (that lacks the LRRs). Magnifying view of NACHT domain illustrates key ATP-binding motifs. (B) The key ATP-binding motifs (from multiple sequence alignment) are boxed in different colors (Walker A: blue; Walker B: salmon; Sensor- 1: orange; PhhCW motif: green; WH-His: purple). The experimentally validated amino acids involved in ATP-binding are shown in red fonts and those not interacting are displayed in green font. (C) Structural overview of NLRP^NACHT models based on OcNOD2 crystal structure (5IRL [41]) (illustrated in different colored cartoons: NLRP1, white; NLRP2, deep salmon; NLRP3, marine; NLRP4, green; NLRP5, violet; NLRP6, orange; NLRP7, hot pink; NLRP8, slate; NLRP9, sand; NLRP10, cyan; NLRP11, dirty violet; NLRP12, forest; NLRP13, green-cyan; and NLRP14, olive) indicate the secondary structural elements (α-helices and β-sheets, which are labeled in white and red fonts within red and yellow boxes, respectively). The ATP/ADP-binding region is displayed in black dotted circle along with the NTP-binding motifs.