2NA1

ULD complex

2NA1 の概要

• エントリーDOI: 10.2210/pdb2na1/pdb
• NMR情報: BMRB: 25923
• 分子名称: Polycomb complex protein BMI-1, Polyhomeotic-like 2 (1 entity in total)
• 機能のキーワード: bmi1, phc2, transcription
• 由来する生物種: mouse, Homo sapiens (Mus musculus, human)
• 細胞内の位置: Nucleus : P35226
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18229.28

構造登録者

Cierpicki, T.,Gray, F.,Cho, H. (登録日: 2015-12-17, 公開日: 2016-11-16, 最終更新日: 2024-05-15)

主引用文献

Gray, F.,Cho, H.J.,Shukla, S.,He, S.,Harris, A.,Boytsov, B.,Jaremko, M.,Jaremko, M.,Demeler, B.,Lawlor, E.R.,Grembecka, J.,Cierpicki, T.
BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.
Nat Commun, 7:13343-13343, 2016

PubMed Abstract: BMI1 is a core component of the polycomb repressive complex 1 (PRC1) and emerging data support a role of BMI1 in cancer. The central domain of BMI1 is involved in protein-protein interactions and is essential for its oncogenic activity. Here, we present the structure of BMI1 bound to the polyhomeotic protein PHC2 illustrating that the central domain of BMI1 adopts an ubiquitin-like (UBL) fold and binds PHC2 in a β-hairpin conformation. Unexpectedly, we find that the UBL domain is involved in homo-oligomerization of BMI1. We demonstrate that both the interaction of BMI1 with polyhomeotic proteins and homo-oligomerization via UBL domain are necessary for H2A ubiquitination activity of PRC1 and for clonogenic potential of U2OS cells. Here, we also emphasize need for joint application of NMR spectroscopy and X-ray crystallography to determine the overall structure of the BMI1-PHC2 complex.

PubMed: 27827373
DOI: 10.1038/ncomms13343

実験手法

SOLUTION NMR