2pqw | pdb_00002pqw

Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form

spinqualitylabelsall models 2pqw, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pqw is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT NonStd Res: MLY Related: 2rjc, 2rjd, 2rje, 2rjf Gene: L3MBTL, KIAA0681, L3MBT (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18. PMID:18026117 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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