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Structure paper

TitlePHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 19, Page 916-924, Year 2012
Publish dateMay 30, 2011 (structure data deposition date)
AuthorsCui, G. / Park, S. / Badeaux, A.I. / Kim, D. / Lee, J. / Thompson, J.R. / Yan, F. / Kaneko, S. / Yuan, Z. / Botuyan, M.V. ...Cui, G. / Park, S. / Badeaux, A.I. / Kim, D. / Lee, J. / Thompson, J.R. / Yan, F. / Kaneko, S. / Yuan, Z. / Botuyan, M.V. / Bedford, M.T. / Cheng, J.Q. / Mer, G.
External linksNat. Struct. Mol. Biol. / PubMed:22864287
MethodsNMR (solution) / X-ray diffraction
Resolution1.928 - 2 Å
Structure data

PDB-2ldm:
Solution structure of human PHF20 Tudor2 domain bound to a p53 segment containing a dimethyllysine analog p53K370me2
Method: SOLUTION NMR

PDB-3p8d:
Crystal structure of the second Tudor domain of human PHF20 (homodimer form)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3sd4:
Crystal structure of the first Tudor domain of human PHF20
Method: X-RAY DIFFRACTION / Resolution: 1.928 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION/PROTEIN BINDING / PHF20 / Tudor domain / Epigenetics / methylated p53 / transcription factor / TRANSCRIPTION-PROTEIN BINDING complex / PROTEIN BINDING / LYSINE-METHYLATED P53 BINDING / HISTONE BINDING / TRANSCRIPTION

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