10.1371/journal.pone.0209420.g004 Jitendra Maharana Jitendra Maharana Debashis Panda Debashis Panda Sachinandan De Sachinandan De Multiple sequence alignment of NACHT domains of NLRPs, NOD1, NOD2 and Nlrc4; the residues interacting with ATP are displayed in bold fonts. 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/Multiple_sequence_alignment_of_NACHT_domains_of_NLRPs_NOD1_NOD2_and_Nlrc4_the_residues_interacting_with_ATP_are_displayed_in_bold_fonts_/7493495 <p>The critical ATP-binding residues (proved experimentally), presented in red-bold font; the residues found within 5-6Å of ATP (adopted from atomic/residual distance calculation; <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0209420#pone.0209420.g004" target="_blank">Fig 4</a>) are visualized in black fonts. The sequence motifs crucial for ATP binding are boxed in different colors (Walker A: blue; Walker B: salmon; Sensor 1: orange; GFxxxxRxxYF motif: light gray; PhhCW motif: green; WH-His: purple). The key ATP-coordinating residues are highlighted in yellow boxes and are marked in inverted triangle.</p>