Fig. 3: Positive patch in the intrinsically disordered region shared with CacOgg. | Communications Biology

Fig. 3: Positive patch in the intrinsically disordered region shared with CacOgg.

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

Fig. 3: Positive patch in the intrinsically disordered region shared with CacOgg.The alt text for this image may have been generated using AI.

a NLRP3 decamer (top) and NLRP3 molecule A (bottom) from PDBID 7pzc. Electrostatic surface potential illustrates the putative DNA binding site in the large positive patch (green arrow). b Sequence alignment of NLRP3 and C. acetobutylicum 8-oxoguanine DNA hydroxylase. Residues important in binding ox-DNA for CacOgg are shown in red. Corresponding residues for NLRP3 are shown in blue. The three-letter amino acid code for residues demonstrated to interact with ox-DNA shown for glycosylase (red) and corresponding for NLRP3 (blue). c Ribbon diagram of CacOgg bound to ox-DNA (left) (protein databank code-3FOZ) and NLRP3 (right) with aligned residues for each protein (red). d The sequence between pyrin and NACHT domains are predicted to contain several intrinsically disordered regions. For simplicity, the rest of the protein containing the LRR domain is not shown. Results from disorder predictor programs are superposed above, color-coded with the key on the right. Intrinsically disordered region (IDR) mapped to NLRP3 3D structure (green arrow in (c)).

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