Fig. 3: dmIR-ECD:DILP5 binding sites. | Nature Communications

Fig. 3: dmIR-ECD:DILP5 binding sites.

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

Fig. 3

a CryoEM reconstruction with model of DILP5 bound in site 1 and 2’; dynamic protomer - in yellow, static – in pink; DILP5 B-chains in blue, A-chains in green. b Ribbon representation of site 1-site 2’ DILP5 binding regions; dynamic/arm-down protomer in green; static protomer in dark yellow, DILP5 B-chains in blue, A-chains in coral, α−CT’ segment in magenta, (*) – FnIII-1’ Lys884-Gly886 loop, (**)—CR Ala594-615Asn loop, (*** red)—FnIII-2’ 1168Ala-1189Ser ledge helix-containing loop. c Site 2’ in dmIR-ECD—colour coding as in (b), human insulin and hIR (PDB ID: 6SOF) in light grey (as in d–f). d A close-up on site 2’ in dmIR-ECD complex showing the DILP5 supporting ledge from the FnIII-2’ domain and putative HBs (dashed lines) that may stabilise this region; colour coding as in (b, c), N atoms in blue, O – in red. e, f Binding of the DILP5 in site 1 down and site 1’; colour coding as above; numbering in grey italic refers to hIR (PDB ID: 6HN5). Superpositions in (c, d) has been done on the respective FnIII-1 domains, and in (e, f) on the L1/L1’ domains without the ligands (see details of the superposition targets in the Supplementary Note 1). Map in (a) was sharpened by B-factor −50 Å2.

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