2x35
From Proteopedia
Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
Structural highlights
FunctionBRPF1_HUMAN Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.[1] [2] 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 PubMedTrimethylation 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
Categories: Homo sapiens | Large Structures | Allen MD | Bonadies N | Bycroft M | Freund SMV | Gottgens B | Huntly BJP | Kvinlaug B | Santiveri CM | Vezzoli A
