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. 2022 Nov 24;13:7216. doi: 10.1038/s41467-022-34865-7

Fig. 6. Conservation of human and M. sexta DUOX and HOCl production.

Fig. 6

a Comparative structures of DUOX in M. sexta and Homo sapiens (DUOX2). b Homology modeling of M. sexta DUOX. The known structure of H. sapiens DUOX1 (left) and model-assisted protein binding site prediction of M. sexta DUOX (right). Regions that were not modeled in the human DUOX1 template structure are also not shown in the model of M. sexta DUOX. c The peroxidase homology domain (PHD) is the active site of HOCl production and is predicted to be highly conserved by model-assisted protein binding site prediction. d DUOX-dependent HOCl production after uracil treatment and its inhibition with diphenyleneiodonium (DPI) but not with N-acetylcysteine (NAC), n = 16, two-tailed t test. Bar charts represent mean and SD. Every data point represents a single animal. Source data are provided as a Source Data file. n = 30, one-way ANOVA, F(3,26) = 3.084, R2 = 0.2624, P = 0.0448. Bar charts represent mean and SD. Every data point represents a single animal. Source data are provided as a Source Data file.