Domain organization, ATP-binding motifs and structural overview of NLRP<sup>NACHT</sup> 3D models.
2018-12-20T18:34:17Z (GMT) by
<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>