4NE3

Human MHF1-MHF2 complex

4NE3 の概要

• エントリーDOI: 10.2210/pdb4ne3/pdb
• 関連するPDBエントリー: 4NDY 4NE1 4NE5 4NE6
• 分子名称: Centromere protein S, Centromere protein X (3 entities in total)
• 機能のキーワード: histone fold, dna repair, genome maintenance, fanconi anemia, fancm, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q8N2Z9 A8MT69
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19185.68

構造登録者

Zhao, Q.,Saro, D.,Sachpatzidis, A.,Sung, P.,Xiong, Y. (登録日: 2013-10-28, 公開日: 2013-12-25, 最終更新日: 2024-11-06)

主引用文献

Zhao, Q.,Saro, D.,Sachpatzidis, A.,Singh, T.R.,Schlingman, D.,Zheng, X.F.,Mack, A.,Tsai, M.S.,Mochrie, S.,Regan, L.,Meetei, A.R.,Sung, P.,Xiong, Y.
The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes.
Nat Commun, 5:2987-2987, 2014

PubMed Abstract: The conserved MHF1-MHF2 (MHF) complex functions in the activation of the Fanconi anaemia pathway of the DNA damage response, in regulating homologous recombination, and in DNA replication fork maintenance. MHF facilitates the processing of multiple types of branched DNAs by the DNA translocase FANCM. Here we report the crystal structure of a human MHF-DNA complex that reveals the DNA-binding mode of MHF. The structure suggests that MHF prefers branched DNA over double-stranded DNA because it engages two duplex arms. Biochemical analyses verify that MHF preferentially engages DNA forks or various four-way junctions independent of the junction-site structure. Furthermore, genetic experiments provide evidence that the observed DNA-binding interface of MHF is important for cellular resistance to DNA damage. These results offer insights into how the MHF complex recognizes branched DNA and stimulates FANCM activity at such a structure to promote genome maintenance.

PubMed: 24390579
DOI: 10.1038/ncomms3987

実験手法

X-RAY DIFFRACTION (1.8007 Å)