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Structure paper

TitleRecognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page 12950-12955, Year 2012
Publish dateDec 16, 2010 (structure data deposition date)
AuthorsArita, K. / Isogai, S. / Oda, T. / Unoki, M. / Sugita, K. / Sekiyama, N. / Kuwata, K. / Hamamoto, R. / Tochio, H. / Sato, M. ...Arita, K. / Isogai, S. / Oda, T. / Unoki, M. / Sugita, K. / Sekiyama, N. / Kuwata, K. / Hamamoto, R. / Tochio, H. / Sato, M. / Ariyoshi, M. / Shirakawa, M.
External linksProc. Natl. Acad. Sci. USA / PubMed:22837395
MethodsX-ray diffraction
Resolution1.41 - 2.904 Å
Structure data

PDB-3ask:
Structure of UHRF1 in complex with histone tail
Method: X-RAY DIFFRACTION / Resolution: 2.904 Å

PDB-3asl:
Structure of UHRF1 in complex with histone tail
Method: X-RAY DIFFRACTION / Resolution: 1.41 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
KeywordsLIGASE/DNA BINDING PROTEIN / histone reader modules / epigenetic regulation / histone H3 / trimethylaion of lysine residue / LIGASE-DNA BINDING PROTEIN complex / histone reader module

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