Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site

@article{Gueneau2013StructureOT,
  title={Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site},
  author={Emeric Gueneau and Claudine Dh{\'e}rin and Pierre Legrand and Carine Tellier-Leb{\`e}gue and Bernard Gilquin and Pierre Bonnesoeur and Floriana Londino and Cathy Quemener and M. Le Du and J A Rivera M{\'a}rquez and Mireille Moutiez and Muriel Gondry and S. Boiteux and Jean Baptiste Charbonnier},
  journal={Nature Structural &Molecular Biology},
  year={2013},
  volume={20},
  pages={461-468}
}
Mismatch-repair factors have a prominent role in surveying eukaryotic DNA-replication fidelity and in ensuring correct meiotic recombination. These functions depend on MutL-homolog heterodimers with Mlh1. In humans, MLH1 mutations underlie half of hereditary nonpolyposis colorectal cancers (HNPCCs). Here we report crystal structures of the MutLα (Mlh1–Pms1 heterodimer) C-terminal domain (CTD) from Saccharomyces cerevisiae, alone and in complex with fragments derived from Mlh1 partners. These… CONTINUE READING
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Structure of the endonuclease domain of MutL : unlicensed to cut

  • M. C. Pillon
  • Mol . Cell
  • 2010

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