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TitleStructure and mechanism of action of the BRCA2 breast cancer tumor suppressor.
Journal, issue, pagesNat Struct Mol Biol, Vol. 21, Issue 11, Page 962-968, Year 2014
Publish dateOct 5, 2014
AuthorsTaha Shahid / Joanna Soroka / Eric Kong / Laurent Malivert / Michael J McIlwraith / Tillman Pape / Stephen C West / Xiaodong Zhang /
PubMed AbstractMutations 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 ...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.
External linksNat Struct Mol Biol / PubMed:25282148 / PubMed Central
MethodsEM (single particle)
Resolution18.5 - 19.5 Å
Structure data

EMDB-2779:
Electron microscopy of human BRCA2 tumour suppressor protein
Method: EM (single particle) / Resolution: 18.5 Å

EMDB-2780:
Electron microscopy of human BRCA2 tumour suppressor bound to human RAD51 recombinase
Method: EM (single particle) / Resolution: 19.5 Å

Source
  • Homo sapiens (human)

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