7XV0

Crystal structure of RPA70N-BLMp1 fusion

7XV0 の概要

• エントリーDOI: 10.2210/pdb7xv0/pdb
• 関連するPDBエントリー: 7XUT
• 分子名称: Replication protein A 70 kDa DNA-binding subunit, Bloom syndrome protein (3 entities in total)
• 機能のキーワード: rpa, rpa70n, blm, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15986.10

構造登録者

Wu, Y.Y.,Zang, N.,Fu, W.M.,Zhou, C. (登録日: 2022-05-20, 公開日: 2023-06-14, 最終更新日: 2024-05-08)

主引用文献

Wu, Y.,Fu, W.,Zang, N.,Zhou, C.
Structural characterization of human RPA70N association with DNA damage response proteins.
Elife, 12:-, 2023

PubMed Abstract: The heterotrimeric Replication protein A (RPA) is the ubiquitous eukaryotic single-stranded DNA (ssDNA) binding protein and participates in nearly all aspects of DNA metabolism, especially DNA damage response. The N-terminal OB domain of the RPA70 subunit (RPA70N) is a major protein-protein interaction element for RPA and binds to more than 20 partner proteins. Previous crystallography studies of RPA70N with p53, DNA2 and PrimPol fragments revealed that RPA70N binds to amphipathic peptides that mimic ssDNA. NMR chemical-shift studies also provided valuable information on the interaction of RPA70N residues with target sequences. However, it is still unclear how RPA70N recognizes and distinguishes such a diverse group of target proteins. Here, we present high-resolution crystal structures of RPA70N in complex with peptides from eight DNA damage response proteins. The structures show that, in addition to the ssDNA mimicry mode of interaction, RPA70N employs multiple ways to bind its partners. Our results advance the mechanistic understanding of RPA70N-mediated recruitment of DNA damage response proteins.

PubMed: 37668474
DOI: 10.7554/eLife.81639

実験手法

X-RAY DIFFRACTION (1.5 Å)