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Structure paper

TitleUHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications.
Journal, issue, pagesEpigenetics, Vol. 4, Page 8-14, Year 2009
Publish dateNov 12, 2008 (structure data deposition date)
AuthorsHashimoto, H. / Horton, J.R. / Zhang, X. / Cheng, X.
External linksPubMed:19077538
MethodsX-ray diffraction
Resolution1.41 - 2.29 Å
Structure data

PDB-3f8i:
Mouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group P21
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-3f8j:
Mouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group C222(1)
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-3fde:
Mouse UHRF1 SRA domain bound with hemi-methylated CpG DNA, crystal structure in space group C222(1) at 1.4 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.41 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-NA:
Unknown entry


ChemComp, No image

ChemComp-UNL:
Unknown ligand

Source
  • mus musculus (house mouse)
KeywordsLIGASE/DNA / UHRF1 / 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 / SRA / SRA domain / DNA CpG methylation

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