Fig. 2: Cryo-EM structure of the IRIns+A62 complex.
From: Functional selectivity of insulin receptor revealed by aptamer-trapped receptor structures
a Half-turn views of the IRA62+Ins structure. Each promotor (orange or green) of the dimer is shown in surface representation or ribbon representation. The A62 aptamer is colored violet and the insulin is colored magenta. b Cartoon representation of the A62 structure. Labels for the modified parts on the 2′ carbon in the ribose sugar (d, f, m) are omitted for clarity. PX and BX represent (5-[N-(1-naphthylmethyl)carboxamide]-2′-deoxyuridine) and (5-[N-benzylcarboxamide]-2′-deoxyuridine), respectively. X is the nucleotide number. The A62-interacting residues are shown; the stacking interactions are shown in pink boxes, base pairings are shown in yellow dots, the FnIII-1′-base interactions are in green boxes, the CR and L2 residue-base interactions are in orange boxes, and the residue-phosphate interactions are in double-lined boxes. c Overall structure of the A62 aptamer. d Close-up view of the A62 bridge across L1 and FnIII-1′ (the blue box in Fig. 2a). e Superimposed structure of the A62 bridge across L1 and FnIII-1′ from IRA62+Ins (blue) and IR2xA62 (red). f, g Close-up view of the binding interface between A62 and IR on f L1 and g FnIII-1′ domains. h, I A62-induced IR phosphorylation (m-pY1150) in CHO-K1 cells expressing WT IR or the indicated point mutants predicted to disturb A62 binding to f L1 or g FnIII-1′ domains. Cells were stimulated with 50 nM A62 for 1 h. The data were representative of three independent experiments. Source data are provided as a Source Data file.
