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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Structure of the single-strand annealing domain of human RAD52 protein.

In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by (i) promoting the annealing of complementary single-stranded DNA and (ii) stimulation of the RAD51 recombinase. The single-strand annealing domain resides in the N-terminal region of the protein and is highly conserved, whereas the nonconserved RAD51-interaction domain is located in the C-terminal region. An N-terminal fragment of human RAD52 (residues 1-209) has been purified to homogeneity and, similar to the full-size protein (residues 1-418), shown to promote single-strand annealing in vitro. We have determined the crystal structure of this single-strand annealing domain at 2.7 A. The structure reveals an undecameric (11) subunit ring with extensive subunit contacts. A large, positively charged groove runs along the surface of the ring, readily suggesting a mechanism by which RAD52 presents the single strand for reannealing with complementary single-stranded DNA.[1]


  1. Structure of the single-strand annealing domain of human RAD52 protein. Singleton, M.R., Wentzell, L.M., Liu, Y., West, S.C., Wigley, D.B. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
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