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

L3MBTL1 recognition of mono- and dimethylated histones.

Author information

1
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
DOI:
10.1038/nsmb1340
[Indexed for MEDLINE]

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