DNA repair: how Ku makes ends meet

Curr Biol. 2001 Nov 13;11(22):R920-4. doi: 10.1016/s0960-9822(01)00555-3.

Abstract

The recently determined crystal structure of the Ku heterodimer, in both DNA-bound and unbound forms, has shed new light on the mechanism by which this protein fulfills its key role in the repair of DNA double-strand breaks.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigens, Nuclear*
  • DNA / chemistry
  • DNA / metabolism
  • DNA Helicases*
  • DNA Repair*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Dimerization
  • Humans
  • Ku Autoantigen
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Nucleic Acid Conformation
  • Protein Structure, Secondary

Substances

  • Antigens, Nuclear
  • DNA-Binding Proteins
  • Nuclear Proteins
  • DNA
  • DNA Helicases
  • XRCC5 protein, human
  • Xrcc6 protein, human
  • Ku Autoantigen