Fig. 2: CryoEM structure of the IM459-bound hIR-Aecto.
From: Activation of the human insulin receptor by non-insulin-related peptides
a NuPAGE 4-12% Bis-Tris gel (non-reducing conditions) of pooled fractions evidencing the presence of the IM459 peptide within the purified complex. This gel experiment was conducted n = 1 times. b Focus-refined cryoEM map showing the fit of IR domains L1, CR, L2, FnIII-1′, and L2′ and the residual density attributable to IM459; density corresponding to domain FnIII-1 is asterisked. c,d Map as in b, showing respective orthogonal views of the rigid-body fit of the co-complex of S519C16 and the hIR L1-CR module (PDB entry 5J3H)12. e-g Comparison of the respective half-structures of the IM459-bound hIR-Aecto, the apo hIR ectodomain (PDB entry 4ZXB), and the four-insulin-bound hIR ectodomain (PDB entry 6SOF), displayed with a common alignment of their respective domains FnIII-1′. In e, the location of domains FnIII-2′ and FnIII-3′ are indicative only. See also Supplementary Fig. 3. In panels b-g, receptor domain colors match those in the primary structure domain layout provided in Supplementary Fig. 2a.
