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2MUR

Solution Structure of the Human FAAP20 UBZ-Ubiquitin Complex

2MUR の概要
エントリーDOI10.2210/pdb2mur/pdb
関連するPDBエントリー2MUQ
NMR情報BMRB: 25230
分子名称Fanconi anemia-associated protein of 20 kDa, Ubiquitin, ZINC ION (3 entities in total)
機能のキーワードubz, faap20, zinc-finger, fanconi anemia, protein binding
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Nucleus: Q6NZ36
Ubiquitin: Cytoplasm . 60S ribosomal protein L40: Cytoplasm : P62987
タンパク質・核酸の鎖数2
化学式量合計13720.96
構造登録者
Wang, S.,Wojtaszek, J.L.,Zhou, P. (登録日: 2014-09-16, 公開日: 2014-12-03, 最終更新日: 2024-05-15)
主引用文献Wojtaszek, J.L.,Wang, S.,Kim, H.,Wu, Q.,D'Andrea, A.D.,Zhou, P.
Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain.
Nucleic Acids Res., 42:13997-14005, 2014
Cited by
PubMed Abstract: FAAP20 is an integral component of the Fanconi anemia core complex that mediates the repair of DNA interstrand crosslinks. The ubiquitin-binding capacity of the FAAP20 UBZ is required for recruitment of the Fanconi anemia complex to interstrand DNA crosslink sites and for interaction with the translesion synthesis machinery. Although the UBZ-ubiquitin interaction is thought to be exclusively encapsulated within the ββα module of UBZ, we show that the FAAP20-ubiquitin interaction extends beyond such a canonical zinc-finger motif. Instead, ubiquitin binding by FAAP20 is accompanied by transforming a disordered tail C-terminal to the UBZ of FAAP20 into a rigid, extended β-loop that latches onto the complex interface of the FAAP20 UBZ and ubiquitin, with the invariant C-terminal tryptophan emanating toward I44(Ub) for enhanced binding specificity and affinity. Substitution of the C-terminal tryptophan with alanine in FAAP20 not only abolishes FAAP20-ubiquitin binding in vitro, but also causes profound cellular hypersensitivity to DNA interstrand crosslink lesions in vivo, highlighting the indispensable role of the C-terminal tail of FAAP20, beyond the compact zinc finger module, toward ubiquitin recognition and Fanconi anemia complex-mediated DNA interstrand crosslink repair.
PubMed: 25414354
DOI: 10.1093/nar/gku1153
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mur
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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