7XGA
NMR strucutre of chimeric protein for model of PHD-Stella complex
Summary for 7XGA
| Entry DOI | 10.2210/pdb7xga/pdb |
| Descriptor | Chimera of E3 ubiquitin-protein ligase UHRF1 and Developmental pluripotency-associated protein 3, ZINC ION (2 entities in total) |
| Functional Keywords | zinc-finger, complex, chimeric model, dna methylation, transcription |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 1 |
| Total formula weight | 14778.11 |
| Authors | Kobayashi, N.,Konuma, T.,Arita, K. (deposition date: 2022-04-04, release date: 2022-12-07, Last modification date: 2024-05-15) |
| Primary citation | Hata, K.,Kobayashi, N.,Sugimura, K.,Qin, W.,Haxholli, D.,Chiba, Y.,Yoshimi, S.,Hayashi, G.,Onoda, H.,Ikegami, T.,Mulholland, C.B.,Nishiyama, A.,Nakanishi, M.,Leonhardt, H.,Konuma, T.,Arita, K. Structural basis for the unique multifaceted interaction of DPPA3 with the UHRF1 PHD finger. Nucleic Acids Res., 50:12527-12542, 2022 Cited by PubMed Abstract: Ubiquitin-like with PHD and RING finger domain-containing protein 1 (UHRF1)-dependent DNA methylation is essential for maintaining cell fate during cell proliferation. Developmental pluripotency-associated 3 (DPPA3) is an intrinsically disordered protein that specifically interacts with UHRF1 and promotes passive DNA demethylation by inhibiting UHRF1 chromatin localization. However, the molecular basis of how DPPA3 interacts with and inhibits UHRF1 remains unclear. We aimed to determine the structure of the mouse UHRF1 plant homeodomain (PHD) complexed with DPPA3 using nuclear magnetic resonance. Induced α-helices in DPPA3 upon binding of UHRF1 PHD contribute to stable complex formation with multifaceted interactions, unlike canonical ligand proteins of the PHD domain. Mutations in the binding interface and unfolding of the DPPA3 helical structure inhibited binding to UHRF1 and its chromatin localization. Our results provide structural insights into the mechanism and specificity underlying the inhibition of UHRF1 by DPPA3. PubMed: 36420895DOI: 10.1093/nar/gkac1082 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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