L3MBTL1 recognition of mono- and dimethylated histones

Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. doi: 10.1038/nsmb1340. Epub 2007 Nov 18.


Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calorimetry
  • Chromosomal Proteins, Non-Histone
  • Histones / metabolism*
  • Lysine / metabolism
  • Methylation
  • Models, Molecular
  • Molecular Sequence Data
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / metabolism*
  • Protein Binding
  • Repressor Proteins
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Proteins


  • Chromosomal Proteins, Non-Histone
  • Histones
  • L3MBTL1 protein, human
  • Neoplasm Proteins
  • Repressor Proteins
  • Tumor Suppressor Proteins
  • Lysine