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TitleThe Arabidopsis (ASHH2) CW domain binds monomethylated K4 of the histone H3 tail through conformational selection.
Journal, issue, pagesFebs J., Vol. 287, Page 4458-4480, Year 2020
Publish dateMar 8, 2019 (structure data deposition date)
AuthorsDobrovolska, O. / Brilkov, M. / Madeleine, N. / Odegard-Fougner, O. / Stromland, O. / Martin, S.R. / De Marco, V. / Christodoulou, E. / Teigen, K. / Isaksson, J. ...Dobrovolska, O. / Brilkov, M. / Madeleine, N. / Odegard-Fougner, O. / Stromland, O. / Martin, S.R. / De Marco, V. / Christodoulou, E. / Teigen, K. / Isaksson, J. / Underhaug, J. / Reuter, N. / Aalen, R.B. / Aasland, R. / Halskau, O.
External linksFebs J. / PubMed:32083791
MethodsNMR (solution)
Structure data

PDB-6qxz:
Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
  • homo sapiens (human)
KeywordsTRANSFERASE / The CW domain of the methyltransferase from Arabidopsis (ASHH2). ASHH2 binds mono- di- and tri-methylated on K4 N-terminal histone tail H3 via CW domain. / PLANT PROTEIN

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