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. 2023 Oct 3;51(5):1789–1800. doi: 10.1042/BST20220741

Figure 4. Other dimeric forms of DNA-PKcs.

Figure 4.

(A) Structure of the apo DNA-PKcs dimer captured in the absence of other NHEJ factors [60]. The interaction site occludes Ku70/80 binding, implying that this state is an inactive form of the kinase. (B) Domain-swap dimer [64]. (C) Closeup of DNA-PK dimer interface in domain-swap dimer. Dimeric interactions are mediated by C-terminal region of Ku80 interacting in trans with NUC194 and M-HEAT regions of opposing DNA-PKcs. (D) Comparison of the same region of interaction in the LR-ATP complex. The interaction site is shifted relative to the DNA-PK dimer, with the NUC194 of each copy of DNA-PKcs interacting with an opposing region of the M-HEAT domain.