L3MBTL1 recognition of mono- and dimethylated histones

被引：156

作者：

Min, Jinrong

Allali-Hassani, Abdellah

Nady, Nataliya

Qi, Chao

Hui Ouyang

Liu, Yongsong

MacKenzie, Farrell

Vedadi, Masoud

Arrowsmith, Cheryl H.

机构：

[1] Univ Toronto, Toronto, ON M5G 1L5, Canada

[2] Huazhong Normal Univ, Coll Life Sci, Wuhan 430079, Peoples R China

[3] Univ Toronto, Ontario Canc Inst, Toronto, ON MG5 1L7, Canada

[4] Univ Toronto, Dept Med Biophys, Toronto, ON MG5 1L7, Canada

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2007年 / 14卷 / 12期

基金：

中国国家自然科学基金; 英国惠康基金; 加拿大创新基金会; 加拿大健康研究院;

关键词：

D O I：

10.1038/nsmb1340

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

收藏

页码：1229 / 1230

页数：2

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