10.1371/journal.pone.0209420.g001 Jitendra Maharana Jitendra Maharana Debashis Panda Debashis Panda Sachinandan De Sachinandan De Domain organization, ATP-binding motifs and structural overview of NLRP<sup>NACHT</sup> 3D models. Public Library of Science 2018 ATP-Mg oligomerization domain NLRP-signaling mechanism ATPase superfamily PRR inflammasome activity sensor-adaptor-effector interactions C-terminal end novel inhibitors NLRP NACHT models residue ATP-binding pocket NLRP-NACHT 3 D models NOD LRR cytosolic pattern recognition receptors bioinformatics approaches ADP mutagenesis data protein modeling AAA pathogen recognition bioinformatics approaches Nucleotide-binding EBD PhhC W motif dynamics simulations G F xxxxRxx Y F motif structural-dynamic features 2018-12-20 18:34:17 Figure https://plos.figshare.com/articles/figure/Domain_organization_ATP-binding_motifs_and_structural_overview_of_NLRP_sup_NACHT_sup_3D_models_/7493486 <p><b>(A)</b> 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>(B)</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. <b>(C)</b> Structural overview of NLRP<sup>NACHT</sup> models based on <i>Oc</i>NOD2 crystal structure (5IRL [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0209420#pone.0209420.ref041" target="_blank">41</a>]) (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.</p>