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TitleStructure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance
Journal, issue, pagesMol. Cell, Vol. 68, Page 350-360.e7, Year 2017
Publish dateDec 28, 2016 (structure data deposition date)
AuthorsIshiyama, S. / Nishiyama, A. / Saeki, Y. / Moritsugu, K. / Morimoto, D. / Yamaguchi, L. / Arai, N. / Matsumura, R. / Kawakami, T. / Mishima, Y. ...Ishiyama, S. / Nishiyama, A. / Saeki, Y. / Moritsugu, K. / Morimoto, D. / Yamaguchi, L. / Arai, N. / Matsumura, R. / Kawakami, T. / Mishima, Y. / Hojo, H. / Shimamura, S. / Ishikawa, F. / Tajima, S. / Tanaka, K. / Ariyoshi, M. / Shirakawa, M. / Ikeguchi, M. / Kidera, A. / Suetake, I. / Arita, K. / Nakanishi, M.
External linksMol. Cell / PubMed:29053958
MethodsX-ray diffraction
Resolution1.997 Å
Structure data

PDB-5wvo:
Crystal structure of DNMT1 RFTS domain in complex with K18/K23 mono-ubiquitylated histone H3
Method: X-RAY DIFFRACTION / Resolution: 1.997 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN/TRANSFERASE / DNA methylation / Ubiquitination / SIGNALING PROTEIN-TRANSFERASE complex

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