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3F8I

Mouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group P21

Summary for 3F8I
Entry DOI10.2210/pdb3f8i/pdb
Related2ZO0 2ZO1 2ZO2 3F8J
DescriptorE3 ubiquitin-protein ligase UHRF1, 5'-D(*DCP*DCP*DAP*DTP*DGP*(5CM)P*DGP*DCP*DTP*DGP*DAP*DC)-3', 5'-D(*DGP*DTP*DCP*DAP*DGP*DCP*DGP*DCP*DAP*DTP*DGP*DG)-3', ... (4 entities in total)
Functional Keywordsuhrf1, base flipping, 5-methylcytosine, cpg methylation, cell cycle, developmental protein, dna damage, dna repair, dna-binding, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation, ubl conjugation pathway, zinc, zinc-finger, ligase-dna complex, ligase/dna
Biological sourceMus musculus (house mouse)
More
Cellular locationNucleus: Q8VDF2
Total number of polymer chains6
Total formula weight62513.04
Authors
Hashimoto, H.,Horton, J.R.,Zhang, X.,Cheng, X. (deposition date: 2008-11-12, release date: 2009-01-06, Last modification date: 2023-09-06)
Primary citationHashimoto, H.,Horton, J.R.,Zhang, X.,Cheng, X.
UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications.
Epigenetics, 4:8-14, 2009
Cited by
PubMed Abstract: Cytosine methylation in DNA is a major epigenetic signal, and plays a central role in propagating chromatin status during cell division. However the mechanistic links between DNA methylation and histone methylation are poorly understood. A multi-domain protein UHRF1 (ubiquitin-like, containing PHD and RING finger domains 1) is required for DNA CpG maintenance methylation at replication forks, and mouse UHRF1-null cells show enhanced susceptibility to DNA replication arrest and DNA damaging agents. Recent data demonstrated that the SET and RING associated (SRA) domain of UHRF1 binds hemimethylated CpG and flips 5-methylcytosine out of the DNA helix, whereas its tandom tudor domain and PHD domain bind the tail of histone H3 in a highly methylation sensitive manner. We hypothesize that UHRF1 brings the two components (histones and DNA) carrying appropriate markers (on the tails of H3 and hemimethylated CpG sites) ready to be assembled into a nucleosome after replication.
PubMed: 19077538
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.29 Å)
Structure validation

243911

數據於2025-10-29公開中

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