1PFB

Structural Basis for specific binding of polycomb chromodomain to histone H3 methylated at K27

1PFB の概要

• エントリーDOI: 10.2210/pdb1pfb/pdb
• 分子名称: Polycomb protein, Histone H3, embryonic, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: chromatin, histone methylation, polycomb, chromodomain, peptide binding protein
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• 細胞内の位置: Nucleus : P26017 P06352
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8174.33

構造登録者

Min, J.R.,Zhang, Y.,Xu, R.-M. (登録日: 2003-05-24, 公開日: 2003-10-07, 最終更新日: 2017-10-11)

主引用文献

Min, J.R.,Zhang, Y.,Xu, R.-M.
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27.
Genes Dev., 17:1823-1828, 2003

PubMed Abstract: The chromodomain of Drosophila Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-A-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.

PubMed: 12897052
DOI: 10.1101/gad.269603

実験手法

X-RAY DIFFRACTION (1.4 Å)