Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18.

L3MBTL1 recognition of mono- and dimethylated histones.

Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH.

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Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario, M5G 1L5, Canada.

Erratum in

Nat Struct Mol Biol. 2008 Jan;15(1):114.

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.

PMID:: 18026117; [PubMed - indexed for MEDLINE]

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Cited by 37 PubMed Central articles

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Structures reported by this article

Crystal Structure Of L3mbtl1 In Complex With H4k20me2 (Residues 12-30), Orthorhombic Form I

PDB: 2RJF

Source: Homo sapiens, synthetic construct

Method: X-Ray Diffraction

Resolution: 2.05 Å

See all 5 structures...

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