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

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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

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 acetyltransferase MOZ/MYST3/KAT6A. In addition to sa...

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Bibliographic Details
Main Authors:	Dreveny, Ingrid, Deeves, Sian E., Fulton, Joel, Yue, Baigong, Messmer, Marie, Bhattacharya, Amit, Collins, Hilary M., Heery, David M.
Format:	Article
Published:	Oxford Journals 2014
Online Access:	https://eprints.nottingham.ac.uk/2594/

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