Autophosphorylation sites revealed
Three-dimensional structural data from crystals of protein kinases have aided the development of drugs and provided insights into kinase regulation and substrate recognition. Many protein kinases trans-autophosphorylate; one kinase phosphorylates another molecule of the same kinase. Anticipating that published crystallographic data may include undescribed information, Xu et al. developed a bioinformatics method to analyze the crystals of kinases for the presence of complexes representing the conformation of kinases during autophosphorylation. The authors identified 15 autophosphorylation complexes in the Protein Data Bank, including five that had not been previously described. With this additional information, structural motifs involved in autophosphorylation become identifiable, which may aid in rational drug design and understanding disease-associated mutations.
