7P0L

Crystal structure of S.pombe Mdb1 BRCT domains in complex with a H2A phosphopeptide

7P0L の概要

• エントリーDOI: 10.2210/pdb7p0l/pdb
• 分子名称: DNA damage response protein Mdb1, Histone H2A-beta (3 entities in total)
• 機能のキーワード: dna damage response, signaling protein
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47876.38

構造登録者

Day, M.,Oliver, A.W.,Pearl, L.H. (登録日: 2021-06-29, 公開日: 2021-12-01, 最終更新日: 2024-11-13)

主引用文献

Day, M.,Oliver, A.W.,Pearl, L.H.
Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.
DNA Repair (Amst), 108:103232-103232, 2021

PubMed Abstract: The cellular response to DNA damage (DDR) that causes replication collapse and/or DNA double strand breaks, is characterised by a massive change in the post-translational modifications (PTM) of hundreds of proteins involved in the detection and repair of DNA damage, and the communication of the state of damage to the cellular systems that regulate replication and cell division. A substantial proportion of these PTMs involve targeted phosphorylation, which among other effects, promotes the formation of multiprotein complexes through the specific binding of phosphorylated motifs on one protein, by specialised domains on other proteins. Understanding the nature of these phosphorylation mediated interactions allows definition of the pathways and networks that coordinate the DDR, and helps identify new targets for therapeutic intervention that may be of benefit in the treatment of cancer, where DDR plays a key role. In this review we summarise the present understanding of how phosphorylated motifs are recognised by BRCT domains, which occur in many DDR proteins. We particularly focus on TOPBP1 - a multi-BRCT domain scaffold protein with essential roles in replication and the repair and signalling of DNA damage.

PubMed: 34678589
DOI: 10.1016/j.dnarep.2021.103232

実験手法

X-RAY DIFFRACTION (1.97 Å)