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. Author manuscript; available in PMC: 2021 Nov 1.
Published in final edited form as: Nature. 2021 Apr 14;593(7858):294–298. doi: 10.1038/s41586-021-03458-7

Extended Data Fig. 3. Comparing the structure of Ku among the LR synaptic complex, the SR synaptic complex, and previously published models.

Extended Data Fig. 3.

a, Ku structure in the LR complex showing outward rotations of both Ku70 and Ku80 vWA domains. b, Crystal structure of XLF KBM bound Ku showing the outward rotation of only Ku80 vWA domain29. c, Crystal structure of apo Ku showing no rotation of either Ku70 or Ku80 vWA domains22. d, Conformation of Ku shown in the cryo-EM structure of apo DNA-PK complex30. Ku70 vWA domain is rotated outward, triggered by binding of DNA-PKcs. e-f, Two copies of XLF KBM bound Ku in the SR complex. The conformation of both copies is the same as the one in the LR complex (a), despite the fact that DNA-PKcs is not present. Color codes for Ku70 and Ku80 are the same as in Fig. 1.