title: L3MBTL1 recognition of mono- and dimethylated histones.
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.
authors.affiliation: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario, M5G 1L5, Canada.
authors.forename: Jinrong
authors.initials: J
authors.lastname: Min
authors.forename: Abdellah
authors.initials: A
authors.lastname: Allali-Hassani
authors.forename: Nataliya
authors.initials: N
authors.lastname: Nady
authors.forename: Chao
authors.initials: C
authors.lastname: Qi
authors.forename: Hui
authors.initials: H
authors.lastname: Ouyang
authors.forename: Yongsong
authors.initials: Y
authors.lastname: Liu
authors.forename: Farrell
authors.initials: F
authors.lastname: MacKenzie
authors.forename: Masoud
authors.initials: M
authors.lastname: Vedadi
authors.forename: Cheryl H
authors.initials: CH
authors.lastname: Arrowsmith
mesh_terms: D000595:Amino Acid Sequence; D002151:Calorimetry; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012097:Repressor Proteins; D017386:Sequence Homology, Amino Acid; D025521:Tumor Suppressor Proteins
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; C120887:L3MBTL1 protein, human; D009363:Neoplasm Proteins; D012097:Repressor Proteins; D025521:Tumor Suppressor Proteins; D008239:Lysine