3V3L

Crystal structure of human RNF146 WWE domain in complex with iso-ADPRibose

3V3L の概要

• エントリーDOI: 10.2210/pdb3v3l/pdb
• 分子名称: E3 ubiquitin-protein ligase RNF146, 2'-O-(5-O-phosphono-alpha-D-ribofuranosyl)adenosine 5'-(dihydrogen phosphate) (3 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytosol: Q9NTX7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21629.09

構造登録者

Wang, Z.,Cheng, Z.,Xu, W. (登録日: 2011-12-13, 公開日: 2012-02-15, 最終更新日: 2024-11-06)

主引用文献

Wang, Z.,Michaud, G.A.,Cheng, Z.,Zhang, Y.,Hinds, T.R.,Fan, E.,Cong, F.,Xu, W.
Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination.
Genes Dev., 26:235-240, 2012

PubMed Abstract: Protein poly(ADP-ribosyl)ation and ubiquitination are two key post-translational modifications regulating many biological processes. Through crystallographic and biochemical analysis, we show that the RNF146 WWE domain recognizes poly(ADP-ribose) (PAR) by interacting with iso-ADP-ribose (iso-ADPR), the smallest internal PAR structural unit containing the characteristic ribose-ribose glycosidic bond formed during poly(ADP-ribosyl)ation. The key iso-ADPR-binding residues we identified are highly conserved among WWE domains. Binding assays further demonstrate that PAR binding is a common function for the WWE domain family. Since many WWE domain-containing proteins are known E3 ubiquitin ligases, our results suggest that protein poly(ADP-ribosyl)ation may be a general mechanism to target proteins for ubiquitination.

PubMed: 22267412
DOI: 10.1101/gad.182618.111

実験手法

X-RAY DIFFRACTION (1.65 Å)