Figure 4. Structures of the insulin and IGF-I receptors and their ligands, and mapping of binding domains.

Figure 4

Structures of the insulin and IGF-I receptors and their ligands, and mapping of binding domains. Left: 3-D structure of the L1CL2 domain of the IGF-I receptor determined by X-ray crystallography. The amino acids determined by alanine scanning mutagenesis to be important for ligand binding are shown in yellow as van der Waals spheres (see text and ref. 65 for details). The 3D structure of the IGF-I molecule201 is shown to scale. The amino acids determined by site-directed mutagenesis to be important for receptor binding are shown in yellow as van der Waals spheres. Since Arg 36 and Arg 37 are lacking in the structure, residues 35 and 38 have been highlighted instead to show approximate location in the middle of the C-peptide domain. Right: The insulin receptor L1-CR-L2 domain has been modelled on the corresponding IGF-I domain coordinates110 using the program SwissModel. The amino acids determined by site-directed mutagenesis to be important for receptor binding are shown in yellow as van der Waals spheres (see text and ref. 65 for details). The 3D structure of the insulin molecule187 is shown to scale. The classical binding surface is shown in yellow as van der Waals spheres; A13 and B17 Leu in the new binding surface are shown in red. Modelling using DS ViewerLite 5.0 (Accelrys). Reprinted with permission from De Meyts P and Whittaker J. Nat Rev Drug Disc 2002; 1:769-783.

From: Insulin and IGF-I Receptor Structure and Binding Mechanism

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