Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 16, Pages 10762-10775Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku729
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Funding
- European Research Council [81500]
- International PhD Projects Programme of the Foundation for Polish Science
- European Union Regional Development Fund [MPD/2009-3/2]
- Foundation of Polish Science [SUB.3/2013]
- Howard Hughes Medical Institute International Early Career Scientist Award [55007428]
- Centre for Preclinical Research and Technology [European Union] [POIG.02.02.00-14-024/08-00]
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Rad2/XPG belongs to the flap nuclease family and is responsible for a key step of the eukaryotic nucleotide excision DNA repair (NER) pathway. To elucidate the mechanism of DNA binding by Rad2/XPG, we solved crystal structures of the catalytic core of Rad2 in complex with a substrate. Rad2 utilizes three structural modules for recognition of the double-stranded portion of DNA substrate, particularly a Rad2-specific alpha-helix for binding the cleaved strand. The protein does not specifically recognize the single-stranded portion of the nucleic acid. Our data suggest that in contrast to related enzymes (FEN1 and EXO1), the Rad2 active site may be more accessible, which would create an exit route for substrates without a free 5' end.
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