5B79
Crystal structure of DPF2 double PHD finger
Summary for 5B79
Entry DOI | 10.2210/pdb5b79/pdb |
Descriptor | Zinc finger protein ubi-d4, ZINC ION (3 entities in total) |
Functional Keywords | dpf2, metal binding protein |
Biological source | Homo sapiens (Human) |
Cellular location | Nucleus: Q92785 |
Total number of polymer chains | 1 |
Total formula weight | 14080.24 |
Authors | |
Primary citation | Xiong, X.,Panchenko, T.,Yang, S.,Zhao, S.,Yan, P.,Zhang, W.,Xie, W.,Li, Y.,Zhao, Y.,Allis, C.D.,Li, H. Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2 Nat.Chem.Biol., 12:1111-1118, 2016 Cited by PubMed Abstract: Recognition of histone covalent modifications by 'reader' modules constitutes a major mechanism for epigenetic regulation. A recent upsurge of newly discovered histone lysine acylations, such as crotonylation (Kcr), butyrylation (Kbu), and propionylation (Kpr), greatly expands the coding potential of histone lysine modifications. Here we demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylations with the strongest preference for Kcr. Crystal structures of the DPF domain of MOZ in complex with H3K14cr, H3K14bu, and H3K14pr peptides reveal that these non-acetyl acylations are anchored in a hydrophobic 'dead-end' pocket with selectivity for crotonylation arising from intimate encapsulation and an amide-sensing hydrogen bonding network. Immunofluorescence and chromatin immunoprecipitation (ChIP)-quantitative PCR (qPCR) showed that MOZ and H3K14cr colocalize in a DPF-dependent manner. Our studies call attention to a new regulatory mechanism centered on histone crotonylation readout by DPF family members. PubMed: 27775714DOI: 10.1038/nchembio.2218 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.601 Å) |
Structure validation
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