2HD5

USP2 in complex with ubiquitin

2HD5 の概要

• エントリーDOI: 10.2210/pdb2hd5/pdb
• 関連するPDBエントリー: 1NB8 1NBF 2AYN 2AYO
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 2, Polyubiquitin, ZINC ION, ... (4 entities in total)
• 機能のキーワード: deubiquitinating protease, cysteine protease, substrate enzyme complex, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm . Isoform 4: Nucleus : O75604
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50065.13

構造登録者

Renatus, M.,Kroemer, M. (登録日: 2006-06-20, 公開日: 2006-08-15, 最終更新日: 2023-08-30)

主引用文献

Renatus, M.,Parrado, S.G.,D'Arcy, A.,Eidhoff, U.,Gerhartz, B.,Hassiepen, U.,Pierrat, B.,Riedl, R.,Vinzenz, D.,Worpenberg, S.,Kroemer, M.
Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2.
Structure, 14:1293-1302, 2006

PubMed Abstract: Deubiquitinating proteases reverse protein ubiquitination and rescue their target proteins from destruction by the proteasome. USP2, a cysteine protease and a member of the ubiquitin specific protease family, is overexpressed in prostate cancer and stabilizes fatty acid synthase, which has been associated with the malignancy of some aggressive prostate cancers. Here, we report the structure of the human USP2 catalytic domain in complex with ubiquitin. Ubiquitin uses two major sites for the interaction with the protease. Both sites are required simultaneously, as shown by USP2 inhibition assays with peptides and ubiquitin mutants. In addition, a layer of ordered water molecules mediates key interactions between ubiquitin and USP2. As several of those molecules are found at identical positions in the previously solved USP7/ubiquitin-aldehyde complex structure, we suggest a general mechanism of water-mediated ubiquitin recognition by USPs.

PubMed: 16905103
DOI: 10.1016/j.str.2006.06.012

実験手法

X-RAY DIFFRACTION (1.85 Å)