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2KVM

Solution structure of the CBX7 chromodomain in complex with a H3K27me2 peptide

Summary for 2KVM
Entry DOI10.2210/pdb2kvm/pdb
NMR InformationBMRB: 16778
DescriptorChromobox protein homolog 7, histone H3 peptide (residues 15-30) with dimethylated lysine 27 (2 entities in total)
Functional Keywordshistone modification, lysine methylation, chromobox, polycomb, chromatin-binding, chromatin regulator, nucleus, repressor, transcription, transcription regulation
Biological sourceMus musculus (mouse)
Total number of polymer chains2
Total formula weight10564.22
Authors
Yap, K.L.,Zeng, L.,Zhou, M. (deposition date: 2010-03-17, release date: 2010-06-30, Last modification date: 2025-03-26)
Primary citationYap, 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: 20541999
DOI: 10.1016/j.molcel.2010.03.021
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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