3c1b | pdb_00003c1b

The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure

spinqualitylabelsall models 3c1b, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3c1b is a 10 chain structure with sequence from Xenopus laevis and Xenopus tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ML3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q28D68_XENTR 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 Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure. The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure.,Lu X, Simon MD, Chodaparambil JV, Hansen JC, Shokat KM, Luger K Nat Struct Mol Biol. 2008 Oct;15(10):1122-4. Epub 2008 Sep 14. PMID:18794842 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone 3D structures

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