1n0w
From Proteopedia
(New page: 200px<br /> <applet load="1n0w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0w, resolution 1.70Å" /> '''Crystal structure o...) |
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| - | [[Image:1n0w.gif|left|200px]]<br /> | + | [[Image:1n0w.gif|left|200px]]<br /><applet load="1n0w" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n0w" size=" | + | |
caption="1n0w, resolution 1.70Å" /> | caption="1n0w, resolution 1.70Å" /> | ||
'''Crystal structure of a RAD51-BRCA2 BRC repeat complex'''<br /> | '''Crystal structure of a RAD51-BRCA2 BRC repeat complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The breast cancer susceptibility protein BRCA2 controls the function of | + | The breast cancer susceptibility protein BRCA2 controls the function of RAD51, a recombinase enzyme, in pathways for DNA repair by homologous recombination. We report here the structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that serves as an interface for oligomerization between individual RAD51 monomers, thus enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. The RAD51 oligomerization motif is highly conserved among RecA-like recombinases, highlighting a common evolutionary origin for the mechanism of nucleoprotein filament formation, mirrored in the BRC repeat. Cancer-associated mutations that affect the BRC repeat disrupt its predicted interaction with RAD51, yielding structural insight into mechanisms for cancer susceptibility. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N0W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, CL and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1N0W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Anand, S.]] | [[Category: Anand, S.]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
[[Category: Lee, M.]] | [[Category: Lee, M.]] | ||
[[Category: Lo, T.]] | [[Category: Lo, T.]] | ||
[[Category: Pellegrini, L.]] | [[Category: Pellegrini, L.]] | ||
| - | [[Category: Venkitaraman, A | + | [[Category: Venkitaraman, A R.]] |
| - | [[Category: Yu, D | + | [[Category: Yu, D S.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: reca-like atpase]] | [[Category: reca-like atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:07 2008'' |
Revision as of 12:01, 21 February 2008
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Crystal structure of a RAD51-BRCA2 BRC repeat complex
Contents |
Overview
The breast cancer susceptibility protein BRCA2 controls the function of RAD51, a recombinase enzyme, in pathways for DNA repair by homologous recombination. We report here the structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that serves as an interface for oligomerization between individual RAD51 monomers, thus enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. The RAD51 oligomerization motif is highly conserved among RecA-like recombinases, highlighting a common evolutionary origin for the mechanism of nucleoprotein filament formation, mirrored in the BRC repeat. Cancer-associated mutations that affect the BRC repeat disrupt its predicted interaction with RAD51, yielding structural insight into mechanisms for cancer susceptibility.
Disease
Known diseases associated with this structure: Breast cancer 2, early onset OMIM:[600185], Breast cancer, male, susceptibility to OMIM:[600185], Breast cancer, susceptibility to OMIM:[179617], Fanconi anemia, complementation group D1 OMIM:[600185], Fanconi anemia, complementation group D2 OMIM:[227646], Pancreatic cancer OMIM:[600185], Prostate cancer OMIM:[600185], Wilms tumor OMIM:[600185]
About this Structure
1N0W is a Protein complex structure of sequences from [1] and Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Insights into DNA recombination from the structure of a RAD51-BRCA2 complex., Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR, Nature. 2002 Nov 21;420(6913):287-93. Epub 2002 Nov 10. PMID:12442171 [[Category: ]]
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