1N0W

Crystal structure of a RAD51-BRCA2 BRC repeat complex

1N0W の概要

• エントリーDOI: 10.2210/pdb1n0w/pdb
• 分子名称: DNA repair protein RAD51 homolog 1, Breast cancer type 2 susceptibility protein, peptide linker, ... (8 entities in total)
• 機能のキーワード: dna repair, homologous recombination, breast cancer susceptibility, reca-like atpase, protein complex, gene regulation-antitumor protein complex, gene regulation/antitumor protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32823.42

構造登録者

Pellegrini, L.,Yu, D.S.,Lo, T.,Anand, S.,Lee, M.,Blundell, T.L.,Venkitaraman, A.R. (登録日: 2002-10-15, 公開日: 2002-11-27, 最終更新日: 2024-11-20)

主引用文献

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

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: 12442171
DOI: 10.1038/nature01230

実験手法

X-RAY DIFFRACTION (1.7 Å)