Polycomb Chromodomain


Polycomb interactions with H3k27me3 peptide


K27me3 usually binds within a hydrophobic pocket formed by three aromatic residues, Tyr 26, Trp 47, and Trp 50. H3K27me3 is shown in cyan and ball and stick model. TRP50, TRP47 and TYR26 are shown in fuchsia, red and green, respectively.

The main-chain carbonyl and amino groups of Lys 23, Ala 24, Ala 25, and Arg 26 of the H3K27me3 peptide make hydrogen bonds with dPC residues 24–28 (located at the N terminus). H3K27me3 is shown in cyan and ball and stick model. Lys 23, Ala 24 and Ala 25 of the H3K27me3 peptide are shown in ball and stick model and green, lime and lightseagreen, respectively. Tyr26, Ala 27, Ala 28 of dPc are shown in ball and stick model and red, maroon and tomato, respectively.

The hydroxyl group of Ser 28 of histone H3 is involved in hydrogen bonding to Glu 58 and Asn 62 of dPc. H3K27me3 is shown in cyan and ball and stick model. Ser 28, Asn 62 and Glu 58 are shown in ball and stick model and green, purple and red, respectively.


Min J, Zhang Y, and  Xu R. 2003. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes & Development. 17(15):1823-8. (PubMed)

1PFB (PDB)

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