Structural basis for the coiled-coil architecture of human CtIP

C. R. Morton, N. J. Rzechorzek, J. D. Maman, M. Kuramochi, H. Sekiguchi, R. Rambo, Y. C. Sasaki, O. R. Davies, L. Pellegrini

Research output: Contribution to journalArticlepeer-review


The DNA repair factor CtIP has a critical function in double-strand break (DSB) repair by homologous recombination, promoting the assembly of the repair apparatus at DNA ends and participating in DNA-end resection. However, the molecular mechanisms of CtIP function in DSB repair remain unclear. Here, we present an atomic model for the three-dimensional architecture of human CtIP, derived from a multi-disciplinary approach that includes X-ray crystallography, small-angle X-ray scattering (SAXS) and diffracted X-ray tracking (DXT). Our data show that CtIP adopts an extended dimer-of-dimers structure, in agreement with a role in bridging distant sites on chromosomal DNA during the recombinational repair. The zinc-binding motif in the CtIP N-terminus alters dynamically the coiled-coil structure, with functional implications for the long-range interactions of CtIP with DNA. Our results provide a structural basis for the three-dimensional arrangement of chains in the CtIP tetramer, a key aspect of CtIP function in DNA DSB repair.
Original languageEnglish
Article number210060
Number of pages12
JournalOpen Biology
Issue number6
Publication statusPublished - 16 Jun 2021


  • human CtIP
  • DNA repair
  • coiled-coil structure


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