3NG2

Crystal structure of the RNF4 ring domain dimer

3NG2 の概要

• エントリーDOI: 10.2210/pdb3ng2/pdb
• 分子名称: RING finger protein 4, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ring domain, e3 ligase, ubiquitylation, sumoylation, zinc-finger, metal binding protein
• 由来する生物種: Rattus norvegicus (rat)
• 細胞内の位置: Cytoplasm: O88846
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16127.99

構造登録者

Liew, C.W.,Day, C.L. (登録日: 2010-06-10, 公開日: 2010-10-06, 最終更新日: 2024-03-20)

主引用文献

Liew, C.W.,Sun, H.,Hunter, T.,Day, C.L.
RING domain dimerization is essential for RNF4 function
Biochem.J., 431:23-29, 2010

PubMed Abstract: RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization.

PubMed: 20681948
DOI: 10.1042/BJ20100957

実験手法

X-RAY DIFFRACTION (1.8 Å)