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TitleThree-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs).
Journal, issue, pagesStructure, Vol. 13, Issue 2, Page 243-255, Year 2005
Publish dateJul 5, 2005
AuthorsAngel Rivera-Calzada / Joseph D Maman / Laura Spagnolo / Laurence H Pearl / Oscar Llorca /
PubMed AbstractDNA-PKcs is a large PI3-kinase-related protein kinase (PIKK) that plays a central role in DNA double-strand break (DSB) repair via nonhomologous end joining. Using cryo-electron microscopy we have ...DNA-PKcs is a large PI3-kinase-related protein kinase (PIKK) that plays a central role in DNA double-strand break (DSB) repair via nonhomologous end joining. Using cryo-electron microscopy we have now generated an approximately 13 A three-dimensional map of DNA-PKcs, revealing the overall architecture and topology of the 4128 residue polypeptide chain and allowing location of domains. The highly conserved C-terminal PIKK catalytic domain forms a central structure from which FAT and FATC domains protrude. Conformational changes observed in these domains on DNA binding suggest that they transduce DNA-induced conformational changes to the catalytic core and regulate kinase activity. The N-terminal segments form long curved tubular-shaped domains based on helical repeats to create interacting surfaces required for macromolecular assembly. Comparison of DNA-PKcs with another PIKK DNA repair factor, ATM, defines a common architecture for this important protein family.
External linksStructure / PubMed:15698568
MethodsEM (single particle)
Resolution13.0 Å
Structure data

EMDB-1102:
Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs).
Method: EM (single particle) / Resolution: 13.0 Å

Source
  • Homo sapiens (human)

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