Fig. 2: CryoEM maps of the dmIR-ECD:DILP5 complex. | Nature Communications

Fig. 2: CryoEM maps of the dmIR-ECD:DILP5 complex.

From: Structural conservation of insulin/IGF signalling axis at the insulin receptors level in Drosophila and humans

Fig. 2

a The initial ligand-free (top/white) and dmIR-ECD:DILP5 complex (bottom/yellow) models from the classification. b The side views of the dmIR-ECD:DILP5 complex; the down ‘dynamic’ protomer is in yellow, and the top ‘static’ protomer in pink; DILP5 B-chains are in blue and A-chains in green. Maps were sharpened by B-factor −50 Å2 (see Methods). c The top and the bottom (from the end of the FnIII-3/3’ domains) views of the dmIR-ECD:DILP5 complex (above and below, respectively). d Ribbon representation of the dmIR-ECD:DILP5 complex; domains are indicated by an abbreviated notation (e.g., FnIII-1 – F1), dynamic protomer - in green, static protomer - in yellow, DILP5s are depicted by spherical atoms, with the B-chains in gold, grey and brown, and the A-chains in blue, coral and pink. S1/1’, S2’ denote DILP5 binding sites 1/1’ and 2’, respectively. The red stars indicate the predicted model of the CR domain Gly491-Cys512 dmIR-specific insert which is not observed in the maps but included here to highlight its possible role in the dmIR.

Back to article page