6KM7

The structural basis for the internal interaction in RBBP5

6KM7 の概要

• エントリーDOI: 10.2210/pdb6km7/pdb
• 分子名称: Retinoblastoma-binding protein 5, SULFATE ION, NONAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: histone methyltransferase, mll1 complex, rbbp5, histone methylation, epigenetics, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 87014.55

構造登録者

Han, J.,Li, T.,Chen, Y. (登録日: 2019-07-31, 公開日: 2019-10-02, 最終更新日: 2024-03-27)

主引用文献

Han, J.,Li, T.,Li, Y.,Li, M.,Wang, X.,Peng, C.,Su, C.,Li, N.,Li, Y.,Xu, Y.,Chen, Y.
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.
Nucleic Acids Res., 47:10426-10438, 2019

PubMed Abstract: The Mixed Lineage Leukemia protein 1 (MLL1) plays an essential role in the maintenance of the histone H3 lysine 4 (H3K4) methylation status for gene expression during differentiation and development. The methyltransferase activity of MLL1 is regulated by three conserved core subunits, WDR5, RBBP5 and ASH2L. Here, we determined the structure of human RBBP5 and demonstrated its role in the assembly and regulation of the MLL1 complex. We identified an internal interaction between the WD40 propeller and the C-terminal distal region in RBBP5, which assisted the maintenance of the compact conformation of the MLL1 complex. We also discovered a vertebrate-specific motif in the C-terminal distal region of RBBP5 that contributed to nucleosome recognition and methylation of nucleosomes by the MLL1 complex. Our results provide new insights into functional conservation and evolutionary plasticity of the scaffold protein RBBP5 in the regulation of KMT2-family methyltransferase complexes.

PubMed: 31544921
DOI: 10.1093/nar/gkz819

実験手法

X-RAY DIFFRACTION (1.801 Å)