1miu: Difference between revisions
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|PDB= 1miu |SIZE=350|CAPTION= <scene name='initialview01'>1miu</scene>, resolution 3.1Å | |PDB= 1miu |SIZE=350|CAPTION= <scene name='initialview01'>1miu</scene>, resolution 3.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1miu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miu OCA], [http://www.ebi.ac.uk/pdbsum/1miu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1miu RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers. | Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: Zheng, N.]] | [[Category: Zheng, N.]] | ||
[[Category: breast cancer susceptibility]] | [[Category: breast cancer susceptibility]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: tumor suppressor]] | [[Category: tumor suppressor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:39 2008'' | ||
