Extended Data Fig. 2: Structural models of kinase-substrate complexes.
From: The intrinsic substrate specificity of the human tyrosine kinome
![Extended Data Fig. 2](https://cdn.statically.io/img/media.springernature.com/full/springer-static/esm/art%3A10.1038%2Fs41586-024-07407-y/MediaObjects/41586_2024_7407_Fig7_ESM.jpg)
a, EGFR (PDB: 2GS6) in complex with synthetic peptide. Dotted green circle shows positive surface potential in the vicinity of the −1 residue. b, Synthetic peptide from its complex with EGFR (PDB: 2GS6) modelled onto ACK (PDB: 1U46). Dotted green circle shows negative surface potential in the vicinity of the −1 residue. c, INSR (PDB: 1IR3) in complex with synthetic peptide. Dotted green circle shows positive surface potential in the vicinity of the substrate N-terminal residues. d, Synthetic peptide from its complex with INSR (PDB: 1IR3) modelled onto DDR2 (PDB: AF-Q16832-K1A)80. Dotted green circle shows negative surface potential in the vicinity of the substrate N-terminal residues. Surface electrostatics are represented with Coulombic potential values were computed in ChimeraX and represented by scale bars (kcal/mol·e). In all panels, “Tyr” represents the site of phosphorylation and “−1” indicates the residue directly to the N-terminal side of the site of phosphorylation.