2X4Y

Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.

Summary for 2X4Y

Entry DOI	10.2210/pdb2x4y/pdb
Related	2D9E 2X35 2X4W 2X4X
Descriptor	PEREGRIN, HISTONE H3.2, SULFATE ION, ... (4 entities in total)
Functional Keywords	transcription, metal-binding, zinc-finger, chromatin regulator, transcription regulation, nucleosome
Biological source	HOMO SAPIENS (HUMAN) More
Cellular location	Nucleus : P55201 Q71DI3
Total number of polymer chains	16
Total formula weight	141315.29
Authors	Vezzoli, A.,Bonadies, N.,Allen, M.D.,Freund, S.M.V.,Santiveri, C.M.,Kvinlaug, B.,Huntly, B.J.P.,Gottgens, B.,Bycroft, M. (deposition date: 2010-02-02, release date: 2010-04-21, Last modification date: 2018-01-24)
Primary citation	Vezzoli, A.,Bonadies, N.,Allen, M.D.,Freund, S.M.V.,Santiveri, C.M.,Kvinlaug, B.,Huntly, B.J.P.,Gottgens, B.,Bycroft, M. Molecular Basis of Histone H3K36Me3 Recognition by the Pwwp Domain of Brpf1. Nat.Struct.Mol.Biol., 17:617-, 2010 Cited by PubMed Abstract: 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. PubMed: 20400950 DOI: 10.1038/NSMB.1797 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation