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BRPF1 蛋白的 PWWP 结构域识别组蛋白 H3K36me3 的分子基础

Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.

机构信息

MRC Centre for Protein Engineering, Cambridge, UK.

出版信息

Nat Struct Mol Biol. 2010 May;17(5):617-9. doi: 10.1038/nsmb.1797. Epub 2010 Apr 18.

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.

摘要

组蛋白 H3 赖氨酸 36 的三甲基化(H3K36me3)协调转录延伸阶段相关事件,并且也是细胞生长和分化的一个重要表观遗传调控因子。我们已经鉴定出含有溴结构域和植物同源结构域(PHD)手指的蛋白 1(BRPF1)的 PWWP 结构域是 H3K36me3 的结合模块,并确定了该结构域与 H3K36me3 衍生肽复合物的结构。

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