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={Georges Mer and Alexey Bochkarev and Rajesh Gupta and Elena Bochkareva and Lori Frappier and C. James Ingles and Aled M. Edwards and Walter J Chazin},
  journal={Cell},
  year={2000},
  volume={103},
  pages={449-456}
}
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