1N0W
Crystal structure of a RAD51-BRCA2 BRC repeat complex
Summary for 1N0W
| Entry DOI | 10.2210/pdb1n0w/pdb |
| Descriptor | DNA repair protein RAD51 homolog 1, Breast cancer type 2 susceptibility protein, peptide linker, ... (8 entities in total) |
| Functional Keywords | dna repair, homologous recombination, breast cancer susceptibility, reca-like atpase, protein complex, gene regulation-antitumor protein complex, gene regulation/antitumor protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 32823.42 |
| Authors | Pellegrini, L.,Yu, D.S.,Lo, T.,Anand, S.,Lee, M.,Blundell, T.L.,Venkitaraman, A.R. (deposition date: 2002-10-15, release date: 2002-11-27, Last modification date: 2024-11-20) |
| Primary citation | Pellegrini, L.,Yu, D.S.,Lo, T.,Anand, S.,Lee, M.,Blundell, T.L.,Venkitaraman, A.R. Insights into DNA recombination from the structure of a RAD51-BRCA2 complex Nature, 420:287-293, 2002 Cited by PubMed Abstract: 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. PubMed: 12442171DOI: 10.1038/nature01230 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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