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. 2008 Oct 16;66(3):407. doi: 10.1007/s00018-008-8303-z

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© Birkhäuser Verlag, Basel 2008

Open Access This is an open access article distributed under the terms of the Creative Commons Attribution Noncommercial License ( https://creativecommons.org/licenses/by-nc/2.0 ), which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.

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Unique substrate recognition properties of two methyl-lysine recognition domains. (A) Space filling representation of the three dimensional structure of the KDM4A tandem-tudor domain in complex with H3K4me3 (magenta) and H4K20me3 (yellow) histone substrates. The N- and C- terminus of the of histone peptides are labelled and the lysine side chain is depicted projecting into the aromatic methyl-lysine recognition cage (cyan). The two unique binding faces of KDM4a appear to permit the dual substrate recognition properties of this methyl lysine binding effector protein. (B) Space filling representation of the RAG2-PHD domain in association with an H3 peptide (green) containing H3K4me3 and H3R2me2s modifications. The methyl-lysine binding aromatic cage is coloured cyan and the Tyr445 residue that interacts with the symmetric dimethyl-arginine is coloured magenta.