Fig. 4: NLRP3 pyrin domain shares fold with human DNA glycosylase. | Communications Biology

Fig. 4: NLRP3 pyrin domain shares fold with human DNA glycosylase.

From: Differential Binding of NLRP3 to non-oxidized and Ox-mtDNA mediates NLRP3 Inflammasome Activation

Fig. 4: NLRP3 pyrin domain shares fold with human DNA glycosylase.The alt text for this image may have been generated using AI.

a Sequence alignment of NLRP3 with human 8-oxoguanine DNA glycosylase (hogg1). Critical amino acids for hogg1 that bind ox-DNA are shown in red and corresponding residues for NLRP3 are in blue. b NLRP3 disease mutations in the pyrin domain and corresponding residues for human glycosylase (hogg1). c Left- topology and fold of NLRP3 (red) for pyrin residues 1–81 superposed with hogg1 bound to ox-DNA (rainbow). From N- to C-terminus, helices 1–5 (H1–H5) have the same fold, including the long loop at the end of H2 (red and green asterisk). Right- super-positioned structure shown with DNA and 8-oxoguanine bound in the active site (green flipped base). Red- NLRP3 1–81 and Rainbow- hOGG1 248-346. d Left- NLRP3 (pink) aligned with hOGG1. NLRP3 Lys2 is not shown in the 3D structure, which starts at Met3. Middle- 3D superposed hogg1 with residues important in binding ox-DNA shown. Right- Superposition of nlrp3 and hogg1 domains shown.

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