Domain organization, ATP-binding motifs and structural overview of NLRPNACHT 3D models.
Figures are generally photos, graphs and static images that would be represented in traditional pdf publications.
(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 NLRPNACHT models based on OcNOD2 crystal structure (5IRL ) (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.