L3MBTL1 recognition of mono- and dimethylated histones.
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Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH
L3MBTL1 recognition of mono- and dimethylated histones.
Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18.
- PubMed ID
- 18026117 [ View in PubMed]
- Abstract
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.