Fig. 5: DILP1 binding site in symmetric dmIR and comparison of dmIR-ligand complexes. | Nature Communications

Fig. 5: DILP1 binding site in symmetric dmIR and comparison of dmIR-ligand complexes.

From: Structure and activation of the Drosophila insulin receptor by three Drosophila insulin-like peptides

Fig. 5: DILP1 binding site in symmetric dmIR and comparison of dmIR-ligand complexes.

a, b Close-up view of the site-1 binding interface of DILP1 to dmIR shown in two views. c Comparison of site-1b binding sites of DILP1 (left), DILP2 (middle) and DILP5 (right) to the FnIII-1′ domain of dmIR. A-chains of DILP molecules are shown as yellow and B-chains as green. FnIII-1 domain of dmIR is shown in blue. d Comparison of FnIII-3 domains of DILP1-dmIR complex with symmetric conformation (left) and DILP5-dmIR complex (right). e Cartoon representation of dmIR/DILP1 complex with symmetric conformation. The two interfaces shown in panels a-d are indicated by dashed boxes with corresponding colors. Two protomers are shown in green and blue. Two DILP1 molecules are shown as yellow. f Representative images of DILP1- or DILP5-induced dmIR autophosphorylation in 293FT cells expressing dmIR wild-type. Cells were treated with 1000 nM DILP1, 100 nM DILP5, or a combination of 1000 nM DILP1 and 100 nM DILP5 for 10 min. Cell lysates were blotted with the indicated antibodies. g Quantification of the western blot data shown in (f). Mean ± sem. N = 4 independent experiments. Statistical significance was determined using 2-way ANOVA. Exact P values are shown in the figure panel. The exact p values are provided in the source data. Source data are provided as a Source data file.

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