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>