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Structure paper

TitleMPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a.
Journal, issue, pagesNat Commun, Vol. 2, Page 533-533, Year 2011
Publish dateJul 12, 2011 (structure data deposition date)
AuthorsChang, Y. / Sun, L. / Kokura, K. / Horton, J.R. / Fukuda, M. / Espejo, A. / Izumi, V. / Koomen, J.M. / Bedford, M.T. / Zhang, X. ...Chang, Y. / Sun, L. / Kokura, K. / Horton, J.R. / Fukuda, M. / Espejo, A. / Izumi, V. / Koomen, J.M. / Bedford, M.T. / Zhang, X. / Shinkai, Y. / Fang, J. / Cheng, X.
External linksNat Commun / PubMed:22086334
MethodsX-ray diffraction
Resolution2.31 - 3.05 Å
Structure data

PDB-3svm:
Human MPP8 - human DNMT3AK47me2 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-3sw9:
GLP (G9a-like protein) SET domain in complex with Dnmt3aK44me0 peptide
Method: X-RAY DIFFRACTION / Resolution: 3.05 Å

PDB-3swc:
GLP (G9a-like protein) SET domain in complex with Dnmt3aK44me2 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.332 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-SFG:
SINEFUNGIN

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsTRANSFERASE / epigenetics / methyl-lysine binding / Chromodomain / The dimethylated human DNMT3AK47me2 is recognized by the chromodomain of MPP8 / MPP8 chromodomain / dimethylated lysine / non-histone lysine methylation / SET domain / protein lysine methyltransferase

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