L3MBTL1 recognition of mono- and dimethylated histones
L3MBTL1 recognition of mono- and dimethylated histones
复制标题
DOI：
10.1038/nsmb1340
复制
发表时间：
2007-12-01
影响因子：
16.8
通讯作者：
Arrowsmith, Cheryl H.
中科院分区：
文献类型：
--
作者：
Min, Jinrong;Allali-Hassani, Abdellah;Arrowsmith, Cheryl H.
L3MBTL1 MBT重复序列与Lys20上二甲基化的组蛋白H4多肽(H4K20me2)形成的复合体的晶体结构表明，三个MBT重复序列中只有第二个MBT重复序列能与单甲基化和双甲基化的组蛋白多肽结合。它的结合口袋与53BP1相似，能够识别组蛋白赖氨酸甲基化的程度。一种意想不到的多肽介导的二聚化模式表明了L3MBTL1对染色质压缩的可能机制。
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.