1h2i
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1h2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2i, resolution 2.7Å" /> '''HUMAN RAD52 PROTEIN,...)
Next diff →
Revision as of 15:05, 12 November 2007
|
HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN
Overview
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.
About this Structure
1H2I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the single-strand annealing domain of human RAD52 protein., Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13492-7. Epub 2002 Oct 7. PMID:12370410
Page seeded by OCA on Mon Nov 12 17:12:00 2007
