5VDC
Crystal structure of the human DPF2 tandem PHD finger domain
Summary for 5VDC
| Entry DOI | 10.2210/pdb5vdc/pdb |
| Descriptor | Zinc finger protein ubi-d4, ZINC ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | histone reader, tandem phd finger, aml, myeloid differentiation, gene regulation |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 14695.93 |
| Authors | Huber, F.M.,Davenport, A.M.,Hoelz, A. (deposition date: 2017-04-01, release date: 2017-05-24, Last modification date: 2024-03-06) |
| Primary citation | 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 Cited by 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: 28533407DOI: 10.1073/pnas.1700328114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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