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. 2021 Jun 7;12:3367. doi: 10.1038/s41467-021-23637-4

Fig. 5. The RDM15 Tudor domain specifically recognizes H3K4me1 and the structure of its complex with the H3K4me1 peptide.

Fig. 5

a Schematic representation of the domain architecture of RDM15. b ITC binding curves between the RDM15 Tudor domain and peptides with different methylation states on the H3K4 site; the curves indicate that RDM15 prefers the H3K4me1 mark over either lower (H3K4me0) or higher (H3K4me2 or H3K4me3) methylation states. NDB no detectable binding. c Overall structure of the RDM15 Tudor domain in complex with the H3K4me1 peptide, with RDM15 shown as cyan ribbon and the peptide shown as stick representation. The composite-omit electron density map at the 1σ level of the bound peptide is shown in a green mesh. d The RDM15 Tudor-H3K4me1 complex with RDM15 shown in an electrostatic surface and the peptide as stick representation. The interaction is mainly mediated by H3R2 and H3K4me1 residues, which insert their side chains in two negatively charged surface grooves of the Tudor domain.