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-Structure paper
Title | Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1 |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 109, Page 12950-12955, Year 2012 |
Publish date | Dec 16, 2010 (structure data deposition date) |
![]() | Arita, 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. |
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Methods | X-ray diffraction |
Resolution | 1.41 - 2.904 Å |
Structure data | ![]() PDB-3ask: ![]() PDB-3asl: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-HOH: ![]() ChemComp-EDO: |
Source |
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![]() | LIGASE/DNA BINDING PROTEIN / histone reader modules / epigenetic regulation / histone H3 / trimethylaion of lysine residue / LIGASE-DNA BINDING PROTEIN complex / histone reader module |