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Fig. 3 | BMC Systems Biology

Fig. 3

From: Investigation and identification of functional post-translational modification sites associated with drug binding and protein-protein interactions

Fig. 3

A case study of the Tyr1131 phosphorylation site associated with drug binding on insulin-like growth factor 1 receptor (IGF1R). The IGF1R is a type of kinases and an inhibitor of the IGF1R could maintain the protein in an inactive conformation. Since the IGF1R was phosphorylated, the crystal structure of its activation loops would be rearranged in such a way that significantly decreases the inhibitor’s affinity. Thus, Tyr1131 phosphorylation site may provide a functional role by modulating the structure of the target protein and reducing the affinity between the inhibitor and the target site

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