8HCU

Crystal structure of BCOR/PCGF1/KDM2B complex

8HCU の概要

• エントリーDOI: 10.2210/pdb8hcu/pdb
• 分子名称: cDNA FLJ55590, highly similar to JmjC domain-containing histone demethylation protein 1B, Polycomb group RING finger protein 1, BCL-6 corepressor, ... (5 entities in total)
• 機能のキーワード: complex, prc1, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 55323.31

構造登録者

Shen, F.,Chen, R.,Xu, J.,Liu, J. (登録日: 2022-11-03, 公開日: 2023-11-15, 最終更新日: 2026-03-04)

主引用文献

Chen, R.,Shen, F.,Zhang, Y.,Sun, M.,Dong, Y.,Yin, Y.,Su, C.,Peng, C.,Liu, J.,Xu, J.
Calcium modulates the tethering of BCOR-PRC1.1 enzymatic core to KDM2B via liquid-liquid phase separation.
Commun Biol, 7:1112-1112, 2024

PubMed Abstract: Recruitment of non-canonical BCOR-PRC1.1 to non-methylated CpG islands via KDM2B plays a fundamental role in transcription control during developmental processes and cancer progression. However, the mechanism is still largely unknown on how this recruitment is regulated. Here, we unveiled the importance of the Poly-D/E regions within the linker of BCOR for its binding to KDM2B. Interestingly, we also demonstrated that these negatively charged Poly-D/E regions on BCOR play autoinhibitory roles in liquid-liquid phase separation (LLPS) of BCOR/PCGF1. Through neutralizing negative charges of these Poly-D/E regions, Ca not only weakens the interaction between BCOR/PCGF1 and KDM2B, but also promotes co-condensation of the enzymatic core of BCOR-PRC1.1 with KDM2B into liquid-like droplet. Accordingly, we propose that Ca could modulate the compartmentation and recruitment of the enzymatic core of BCOR-PRC1.1 on KDM2B target loci. Thus, our finding advances the mechanistic understanding on how the tethering of BCOR-PRC1.1 enzymatic core to KDM2B is regulated.

PubMed: 39256555
DOI: 10.1038/s42003-024-06820-3

実験手法

X-RAY DIFFRACTION (2.2 Å)