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TitleYng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
Journal, issue, pagesMol. Cell, Vol. 24, Page 785-796, Year 2006
Publish dateNov 15, 2006 (structure data deposition date)
AuthorsTaverna, S.D. / Ilin, S. / Rogers, R.S. / Tanny, J.C. / Lavender, H. / Li, H. / Baker, L. / Boyle, J. / Blair, L.P. / Chait, B.T. ...Taverna, S.D. / Ilin, S. / Rogers, R.S. / Tanny, J.C. / Lavender, H. / Li, H. / Baker, L. / Boyle, J. / Blair, L.P. / Chait, B.T. / Patel, D.J. / Aitchison, J.D. / Tackett, A.J. / Allis, C.D.
External linksMol. Cell / PubMed:17157260
MethodsNMR (solution)
Structure data

PDB-2jmi:
NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state
Method: SOLUTION NMR

PDB-2jmj:
NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN BINDING / PHD / Histone / Recognition / Yeast / H3K4me3 / complex

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