| Literature DB >> 18026117 |
Jinrong Min1, Abdellah Allali-Hassani, Nataliya Nady, Chao Qi, Hui Ouyang, Yongsong Liu, Farrell MacKenzie, Masoud Vedadi, Cheryl H Arrowsmith.
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.Entities:
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Year: 2007 PMID： 18026117 DOI： 10.1038/nsmb1340
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369