In this section
@article{Shahid:2014:10.1038/nsmb.2899,
author = {Shahid, T and Soroka, J and Kong, EH and Malivert, L and McIlwraith, MJ and Pape, T and West, SC and Zhang, X},
doi = {10.1038/nsmb.2899},
journal = {Nature Structural and Molecular Biology},
pages = {962--968},
title = {Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor},
url = {http://dx.doi.org/10.1038/nsmb.2899},
volume = {21},
year = {2014}
}
TY - JOUR
AB - Mutations in BRCA2 increase susceptibility to breast, ovarian and prostate cancers. The product of human BRCA2, BRCA2 protein, has a key role in the repair of DNA double-strand breaks and interstrand cross-links by RAD51-mediated homologous recombination. Here, we present a biochemical and structural characterization of full-length (3,418 amino acid) BRCA2, alone and in complex with RAD51. We show that BRCA2 facilitates nucleation of RAD51 filaments at multiple sites on single-stranded DNA. Three-dimensional EM reconstructions revealed that BRCA2 exists as a dimer and that two oppositely oriented sets of RAD51 molecules bind the dimer. Single-stranded DNA binds along the long axis of BRCA2, such that only one set of RAD51 monomers can form a productive complex with DNA and establish filament formation. Our data define the molecular mechanism by which this tumor suppressor facilitates RAD51-mediated homologous-recombinational repair.
AU - Shahid,T
AU - Soroka,J
AU - Kong,EH
AU - Malivert,L
AU - McIlwraith,MJ
AU - Pape,T
AU - West,SC
AU - Zhang,X
DO - 10.1038/nsmb.2899
EP - 968
PY - 2014///
SN - 1545-9985
SP - 962
TI - Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor
T2 - Nature Structural and Molecular Biology
UR - http://dx.doi.org/10.1038/nsmb.2899
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000344513400005&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://www.nature.com/articles/nsmb.2899
VL - 21
ER -
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