Fig. 1: The structural domains of DNA-PKcs—HEAT, FAT, FRB, kinase, and FATC—and prominent phosphorylation clusters. | npj Precision Oncology

Fig. 1: The structural domains of DNA-PKcs—HEAT, FAT, FRB, kinase, and FATC—and prominent phosphorylation clusters.

From: Secrets of DNA-PKcs beyond DNA repair

Fig. 1

HEAT repeats facilitate binding with DNA and are potentially involved in protein-protein interactions. The FAT and FATC domains mediate the activity of the kinase domain and act as a sensor during the activation of DNA-PKcs. The kinase region is the catalytic region that phosphorylates target ser/thr residues. Within the kinase domain, FRB is speculated to be a “gatekeeper” which further regulates the activity of the protein. Prominent phosphorylation clusters, PQR and ABCDE, are important for the activation and function of DNA-PKcs. Figure created with BioRender.com.

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