2qqs | pdb_00002qqs

JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide

spinqualitylabelsall models 2qqs, resolution 2.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qqs is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: M3L Related: 2qqr Gene: JMJD2A, JHDM3A, JMJD2, KIAA0677 (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 The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.,Lee J, Thompson JR, Botuyan MV, Mer G Nat Struct Mol Biol. 2008 Jan;15(1):109-11. Epub 2007 Dec 16. PMID:18084306 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Jumonji domain-containing protein 2A

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