7LDG

Crystal structure of the MEILB2-BRCA2 complex

7LDG の概要

• エントリーDOI: 10.2210/pdb7ldg/pdb
• 分子名称: Heat shock factor 2-binding protein, Breast cancer type 2 susceptibility protein (3 entities in total)
• 機能のキーワード: complex, recruiter, protein-protein interaction, armadillo-repeat, recombination
• 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: 72087.28

構造登録者

Nandakumar, J.,Pendlebury, D.F. (登録日: 2021-01-13, 公開日: 2021-08-11, 最終更新日: 2024-10-23)

主引用文献

Pendlebury, D.F.,Zhang, J.,Agrawal, R.,Shibuya, H.,Nandakumar, J.
Structure of a meiosis-specific complex central to BRCA2 localization at recombination sites.
Nat.Struct.Mol.Biol., 28:671-680, 2021

PubMed Abstract: Meiotic cells invoke breast cancer susceptibility gene 2 (BRCA2) to repair programmed double-stranded DNA breaks and accomplish homologous recombination. The meiosis-specific protein MEILB2 facilitates BRCA2 recruitment to meiotic recombination sites. Here, we combine crystallography, biochemical analysis and a mouse meiosis model to reveal a robust architecture that ensures meiotic BRCA2 recruitment. The crystal structure of the MEILB2-BRCA2 complex reveals how two MEILB2 homodimers sandwich two chains of BRCA2 to afford a 4:2 architecture. The sandwich lacks close contact between the two MEILB2 dimers or the two BRCA2 chains. Instead, the two halves of each BRCA2 chain bridge two MEILB2 subunits from different homodimers to form the MEILB2-BRCA2-MEILB2 sandwich. Several identical residues from the two MEILB2 subunits are employed to engage the BRCA2 halves, justifying their strict conservation. Mutational analysis of the interface reveals a synergistic mechanism for MEILB2-BRCA2 recruitment during meiosis. Overall, these studies demonstrate how BRCA2 efficiently localizes in the cell to facilitate meiosis.

PubMed: 34373645
DOI: 10.1038/s41594-021-00635-0

実験手法

X-RAY DIFFRACTION (2.56 Å)