Fig. 5: Superposition of the dmIR-ECD:DILP5 dynamic and static protomers on the corresponding protomers of representative human insulin:IR complexes. | Nature Communications

Fig. 5: Superposition of the dmIR-ECD:DILP5 dynamic and static protomers on the corresponding protomers of representative human insulin:IR complexes.

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

Fig. 5

a dmIR-ECD dynamic protomers are in green and the static protomers in (b) are in yellow; human protomers are in white with their respective PDB IDs; DILP5 B-chain in blue, A-chain in coral; Îħ-CT in magenta; black diagrams depict the number of insulins/protomer in the respective human complexes and the site of binding. All protomers were superposed in Coot (72) LSQ option on CÎħ atoms of the FnIII-1 domains (Ala807-Ans925 in dmIR on Glu471-Asp591 in hIR). The 827-847 and 881-887 loops in dmIR-ECD were removed prior to the superposition to minimise their potentially misleading bias in the superposition of a very similar cores of these domains (see Supplementary Note 1 for the exact targets). Two stars indicate ECD derived from the full-length IR models, one star—ECD from Leu-zipper containing ECD hIR, no star—ECD-only determined structure.

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