2x35 | pdb_00002x35

MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP DOMAIN OF BRPF1.

spinqualitylabelsall models 2x35, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x35 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2d9e 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 Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger-containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide. Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.,Vezzoli A, Bonadies N, Allen MD, Freund SM, Santiveri CM, Kvinlaug BT, Huntly BJ, Gottgens B, Bycroft M Nat Struct Mol Biol. 2010 May;17(5):617-9. Epub 2010 Apr 18. PMID:20400950 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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