抄録
The Rad52 protein and its homologs play critical roles in eukaryotic homologous recombination. In the present study, we have determined the crystal structure of the N-terminal, homologouspairing domain of Rad52. The structure revealed an undecameric ring that has an exposed groove essential for DNA binding. Amino acid residues inside the groove are directly involved in DNA binding as evidenced by mutational analyses.
