Summary information and primary citation
- PDB-id
- 8gpn; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- gene regulation
- Method
- cryo-EM (3.2 Å)
- Summary
- Human menin in complex with h3k79me2 nucleosome
- Reference
- Lin J, Wu Y, Tian G, Yu D, Yang E, Lam WH, Liu Z, Jing Y, Dang S, Bao X, Wong JWH, Zhai Y, Li XD (2023): "Menin "reads" H3K79me2 mark in a nucleosomal context." Science, 379, 717-723. doi: 10.1126/science.adc9318.
- Abstract
- Methylation of histone H3 lysine-79 (H3K79) is an epigenetic mark for gene regulation in development, cellular differentiation, and disease progression. However, how this histone mark is translated into downstream effects remains poorly understood owing to a lack of knowledge about its readers. We developed a nucleosome-based photoaffinity probe to capture proteins that recognize H3K79 dimethylation (H3K79me2) in a nucleosomal context. In combination with a quantitative proteomics approach, this probe identified menin as a H3K79me2 reader. A cryo-electron microscopy structure of menin bound to an H3K79me2 nucleosome revealed that menin engages with the nucleosome using its fingers and palm domains and recognizes the methylation mark through a π-cation interaction. In cells, menin is selectively associated with H3K79me2 on chromatin, particularly in gene bodies.
