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TitleStructure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations.
Journal, issue, pagesPlos One, Vol. 8, Page e83737-e83737, Year 2013
Publish dateAug 30, 2013 (structure data deposition date)
AuthorsWu, H. / Zeng, H. / Dong, A. / Li, F. / He, H. / Senisterra, G. / Seitova, A. / Duan, S. / Brown, P.J. / Vedadi, M. ...Wu, H. / Zeng, H. / Dong, A. / Li, F. / He, H. / Senisterra, G. / Seitova, A. / Duan, S. / Brown, P.J. / Vedadi, M. / Arrowsmith, C.H. / Schapira, M.
External linksPlos One / PubMed:24367611
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-4mi0:
Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-UNX:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / EZH2 / Gene regulation / chromatin modification / histone methyltransferase / transcription / gene silencing / Polycomb Repressive Complex 2 / Structural Genomics / Structural Genomics Consortium / SGC

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