Structural Basis for the Recognition of DNA Repair Proteins UNG2, XPA, and RAD52 by Replication Factor RPA

@article{Mer2000StructuralBF,
  title={Structural Basis for the Recognition of DNA Repair Proteins UNG2, XPA, and RAD52 by Replication Factor RPA},
  author={G. Mer and A. Bochkarev and R. Gupta and E. Bochkareva and L. Frappier and C.James Ingles and A. Edwards and W. Chazin},
  journal={Cell},
  year={2000},
  volume={103},
  pages={449-456}
}
  • G. Mer, A. Bochkarev, +5 authors W. Chazin
  • Published 2000
  • Medicine, Biology
  • Cell
  • Replication protein A (RPA), the nuclear ssDNA-binding protein in eukaryotes, is essential to DNA replication, recombination, and repair. We have shown that a globular domain at the C terminus of subunit RPA32 contains a specific surface that interacts in a similar manner with the DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which functions in a different repair pathway. NMR structures of the RPA32 domain, free and in complex with the minimal interaction domain of UNG2, were… CONTINUE READING

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