2KVM
Solution structure of the CBX7 chromodomain in complex with a H3K27me2 peptide
Summary for 2KVM
Entry DOI | 10.2210/pdb2kvm/pdb |
NMR Information | BMRB: 16778 |
Descriptor | Chromobox protein homolog 7, histone H3 peptide (residues 15-30) with dimethylated lysine 27 (2 entities in total) |
Functional Keywords | histone modification, lysine methylation, chromobox, polycomb, chromatin-binding, chromatin regulator, nucleus, repressor, transcription, transcription regulation |
Biological source | Mus musculus (mouse) |
Total number of polymer chains | 2 |
Total formula weight | 10564.22 |
Authors | |
Primary citation | Yap, K.L.,Li, S.,Munoz-Cabello, A.M.,Raguz, S.,Zeng, L.,Mujtaba, S.,Gil, J.,Walsh, M.J.,Zhou, M.M. Molecular interplay of the noncoding RNA ANRIL and methylated histone H3 lysine 27 by polycomb CBX7 in transcriptional silencing of INK4a. Mol.Cell, 38:662-674, 2010 Cited by PubMed Abstract: Expression of the INK4b/ARF/INK4a tumor suppressor locus in normal and cancerous cell growth is controlled by methylation of histone H3 at lysine 27 (H3K27me) as directed by the Polycomb group proteins. The antisense noncoding RNA ANRIL of the INK4b/ARF/INK4a locus is also important for expression of the protein-coding genes in cis, but its mechanism has remained elusive. Here we report that chromobox 7 (CBX7) within the polycomb repressive complex 1 binds to ANRIL, and both CBX7 and ANRIL are found at elevated levels in prostate cancer tissues. In concert with H3K27me recognition, binding to RNA contributes to CBX7 function, and disruption of either interaction impacts the ability of CBX7 to repress the INK4b/ARF/INK4a locus and control senescence. Structure-guided analysis reveals the molecular interplay between noncoding RNA and H3K27me as mediated by the conserved chromodomain. Our study suggests a mechanism by which noncoding RNA participates directly in epigenetic transcriptional repression. PubMed: 20541999DOI: 10.1016/j.molcel.2010.03.021 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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