Figure 1
From: Role of Methoprene-tolerant in the regulation of oogenesis in Dipetalogaster maxima
DmaxMet structure, modelling and docking. (a) Schematic view of DmaxMet1 (713 aa) and DmaxMet2 (676 aa) predicted protein sequences, showing the conserved domains, as well as DNA and ligand binding locations. (b) Structural model for DmaxMet1, displayed as a molecular surface superposed to a cartoon representation (left), with the detail of the in silico interactions between JHSB3 and the PAS-B domain of DmaxMet1 (right). (c) Alignment of DmaxMet1 PAS-B-PAC domains and D. melanogaster Met (NP_001285132.1), T. castaneum Met (NP_001092812.1), and A. aegypti Met (AAX55681.1), showing amino acid (aa) residues involved in JH-Met interactions. Gray line: amino acids (aa) position of DmaxMet; black bolded amino acids: aa affecting JH binding to DmaxMet1; shaded blue amino acids: mutations that affected JH binding to D. melanogaster Met, T. castaneum Met or A. aegypti Met; red amino acids: aa identified by docking or modelling as relevant for JH binding.
