期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 14, 期 12, 页码 1229-1230出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1340
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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.
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