5VDC

Crystal structure of the human DPF2 tandem PHD finger domain

5VDC の概要

• エントリーDOI: 10.2210/pdb5vdc/pdb
• 分子名称: Zinc finger protein ubi-d4, ZINC ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: histone reader, tandem phd finger, aml, myeloid differentiation, gene regulation
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14695.93

構造登録者

Huber, F.M.,Davenport, A.M.,Hoelz, A. (登録日: 2017-04-01, 公開日: 2017-05-24, 最終更新日: 2024-03-06)

主引用文献

Huber, F.M.,Greenblatt, S.M.,Davenport, A.M.,Martinez, C.,Xu, Y.,Vu, L.P.,Nimer, S.D.,Hoelz, A.
Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.
Proc. Natl. Acad. Sci. U.S.A., 114:6016-6021, 2017

PubMed Abstract: Double plant homeodomain finger 2 (DPF2) is a highly evolutionarily conserved member of the d4 protein family that is ubiquitously expressed in human tissues and was recently shown to inhibit the myeloid differentiation of hematopoietic stem/progenitor and acute myelogenous leukemia cells. Here, we present the crystal structure of the tandem plant homeodomain finger domain of human DPF2 at 1.6-Å resolution. We show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via bipartite binding pockets on the DPF2 surface. Blocking these interactions through targeted mutagenesis of DPF2 abolishes its recruitment to target chromatin regions as well as its ability to prevent myeloid differentiation in vivo. Our findings suggest that the histone binding of DPF2 plays an important regulatory role in the transcriptional program that drives myeloid differentiation.

PubMed: 28533407
DOI: 10.1073/pnas.1700328114

実験手法

X-RAY DIFFRACTION (1.6 Å)