Structure of the single-strand break repair protein XRCC1
1. ARTICLE LINKS
Figures and
tables
SEE ALSO
News and Views
by Rice
ARTICLE TOOLS
Send to a friend
Export citation
Export
references
Rights and
permissions
Order
commercial
reprints
SEARCH
PUBMED FOR
Assen
Marintchev
Mary A. Mullen
Mark W.
Maciejewski
Borlan Pan
Michael R. Gryk
Gregory P.
Mullen
more authors of
this article
Access
To read this story in full you will need to login or make a payment
(see right).
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.
To read this story in full you will need to
login or make a payment (see right).
Nature Structural & Molecular Biology ISSN 1545-9993 EISSN 1545-9985
About us
Contact us
Privacy policy
Use of cookies
Naturejobs
Nature Asia
Access : Solution structure of the single-strand break repair protein XRC... http://www.nature.com/nsmb/journal/v6/n9/full/nsb0999_884.html
1 of 2 8/10/2016 7:36 PM