3IXS

Ring1B C-terminal domain/RYBP C-terminal domain Complex

3IXS の概要

• エントリーDOI: 10.2210/pdb3ixs/pdb
• 関連するPDBエントリー: 3GS2
• 分子名称: E3 ubiquitin-protein ligase RING2, RING1 and YY1-binding protein, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: ring1b, rybp, polycomb, e3-ligase, chromosomal protein, transcription regulation, chromatin regulator, transcription repressor, ligase, metal-binding, nucleus, phosphoprotein, repressor, transcription, ubl conjugation pathway, zinc-finger, apoptosis, dna-binding, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus (By similarity): Q99496; Nucleus: Q8N488
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 100786.96

構造登録者

Wang, R.,Taylor, A.B.,Kim, C.A. (登録日: 2009-09-04, 公開日: 2010-08-25, 最終更新日: 2024-02-21)

主引用文献

Wang, R.,Taylor, A.B.,Leal, B.Z.,Chadwell, L.V.,Ilangovan, U.,Robinson, A.K.,Schirf, V.,Hart, P.J.,Lafer, E.M.,Demeler, B.,Hinck, A.P.,McEwen, D.G.,Kim, C.A.
Polycomb Group Targeting through Different Binding Partners of RING1B C-Terminal Domain.
Structure, 18:966-975, 2010

PubMed Abstract: RING1B, a Polycomb Group (PcG) protein, binds methylated chromatin through its association with another PcG protein called Polycomb (Pc). However, RING1B can associate with nonmethylated chromatin suggesting an alternate mechanism for RING1B interaction with chromatin. Here, we demonstrate that two proteins with little sequence identity between them, the Pc cbox domain and RYBP, bind the same surface on the C-terminal domain of RING1B (C-RING1B). Pc cbox and RYBP each fold into a nearly identical, intermolecular beta sheet with C-RING1B and a loop structure which are completely different in the two proteins. Both the beta sheet and loop are required for stable binding and transcription repression. Further, a mutation engineered to disrupt binding on the Drosophila dRING1 protein prevents chromatin association and PcG function in vivo. These results suggest that PcG targeting to different chromatin locations relies, in part, on binding partners of C-RING1B that are diverse in sequence and structure.

PubMed: 20696397
DOI: 10.1016/j.str.2010.04.013

実験手法

X-RAY DIFFRACTION (1.7 Å)