4hcz | pdb_00004hcz

PHF1 Tudor in complex with H3K36me3

spinqualitylabelsall models 4hcz, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hcz 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. Method: X-ray diffraction, Resolution 1.85Å Ligands: M3L Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHF1_HUMAN Transcriptional repressor. May promote methylation of histone H3 on 'Lys-27' by the PRC2/EED-EZH2 complex. Publication Abstract from PubMed The PHD finger protein 1 (PHF1) is essential in epigenetic regulation and genome maintenance. Here we show that the Tudor domain of human PHF1 binds to histone H3 trimethylated at Lys36 (H3K36me3). We report a 1.9-A resolution crystal structure of the Tudor domain in complex with H3K36me3 and describe the molecular mechanism of H3K36me3 recognition using NMR. Binding of PHF1 to H3K36me3 inhibits the ability of the Polycomb PRC2 complex to methylate Lys27 of histone H3 in vitro and in vivo. Laser microirradiation data show that PHF1 is transiently recruited to DNA double-strand breaks, and PHF1 mutants impaired in the H3K36me3 interaction exhibit reduced retention at double-strand break sites. Together, our findings suggest that PHF1 can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1.,Musselman CA, Avvakumov N, Watanabe R, Abraham CG, Lalonde ME, Hong Z, Allen C, Roy S, Nunez JK, Nickoloff J, Kulesza CA, Yasui A, Cote J, Kutateladze TG Nat Struct Mol Biol. 2012 Dec;19(12):1266-72. doi: 10.1038/nsmb.2435. Epub 2012, Nov 11. PMID:23142980 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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