Crystal Structure of a G:T/U Mismatch-Specific DNA Glycosylase Mismatch Recognition by Complementary-Strand Interactions

@article{Barrett1998CrystalSO,
  title={Crystal Structure of a G:T/U Mismatch-Specific DNA Glycosylase Mismatch Recognition by Complementary-Strand Interactions},
  author={T. Barrett and R. Savva and G. Panayotou and T. Barlow and T. Brown and J. Jiricny and L. Pearl},
  journal={Cell},
  year={1998},
  volume={92},
  pages={117-129}
}
  • T. Barrett, R. Savva, +4 authors L. Pearl
  • Published 1998
  • Biology, Medicine
  • Cell
  • G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG… CONTINUE READING
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