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PUBMED FOR
Assen
Marintchev
Mary A. Mullen
Mark W.
Maciejewski
Borlan Pan
Michael R. Gryk
Gregory P.
Mullen
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Article
Nature Structural & Molecular Biology 6, 884 - 893 (1999)
doi:10.1038/12347
Solution structure of the single-
strand break repair protein
XRCC1 N-terminal domain
Assen Marintchev1, Mary A. Mullen1, Mark W.
Maciejewski1, Borlan Pan1, Michael R. Gryk1 &
Gregory P. Mullen1
XRCC1 functions in the repair of single-
strand DNA breaks in mammalian cells and
forms a repair complex with -Pol, ligase III
and PARP. Here we describe the NMR
solution structure of the XRCC1 N-terminal
domain (XRCC1 NTD). The structural core is
a -sandwich with -strands connected by
loops, three helices and two short
two-stranded -sheets at each connection
side. We show, for the first time, that the
XRCC1 NTD specifically binds single-strand
break DNA (gapped and nicked). We also
show that the XRCC1 NTD binds a gapped
DNA– -Pol complex. The DNA binding and
-Pol binding surfaces were mapped by NMR
and found to be well suited for interaction
with single-strand gap DNA containing a 90°
bend, and for simultaneously making
contacts with the palm-thumb of -Pol in a
ternary complex. The findings suggest a
mechanism for preferential binding of the
XRCC1 NTD to flexible single-strand break
DNA.
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Nature Structural & Molecular Biology ISSN 1545-9993 EISSN 1545-9985
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