The double PHD finger domain of MOZ/MYST3 induces ?-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification
(2014)
Journal Article
Dreveny, I., Deeves, S. E., Fulton, J., Yue, B., Messmer, M., Bhattacharya, A., …Heery, D. M. (2014). The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Research, 42(2), 822-835. https://doi.org/10.1093/nar/gkt931
Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine ac... Read More about The double PHD finger domain of MOZ/MYST3 induces ?-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.