Figure_2.tif (1.27 MB)
hMPP8 chromodomain specifically recognizes di- and tri- methylated H3K9 peptides.
figure
posted on 2011-10-12, 01:35 authored by Jing Li, Zhihong Li, Jianbin Ruan, Chao Xu, Yufeng Tong, Patricia W. Pan, Wolfram Tempel, Lissete Crombet, Jinrong Min, Jianye Zang(A) and (B) Binding affinity of hMPP8 chromodomain to di- and tri-methylated H3K9 peptides was measured by SPR method (C) Overall structures of hMPP8 chromodomain in complex with histone H3K9me3 peptide. Cyan and green: hMPP8 chromodomain, yellow and magenta: methylated histone H3K9 peptide. (D) Monomer structure of hMPP8 chromodomain in complex with histone H3K9me3 peptides. Cyan: hMPP8 chromodomain, yellow: histone H3K9me3 peptide. (E) Interactions between hMPP8 chromodomain and H3K9me3 peptide. The chromodomain is shown in cartoon representation and colored in cyan. The H3K9me3 peptide is shown in a stick mode. (F) The aromatic cage accommodating trimethylated lysine 9.
