4O62

CW-type zinc finger of ZCWPW2 in complex with the amino terminus of histone H3

4O62 の概要

• エントリーDOI: 10.2210/pdb4o62/pdb
• 分子名称: Zinc finger CW-type PWWP domain protein 2, Histone H3.3, ZINC ION, ... (5 entities in total)
• 機能のキーワード: zinc finger, histone, structural genomics, structural genomics consortium, sgc, metal-dna binding protein complex, metal/dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Chromosome . Nucleus : K7ES00
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 22725.94

構造登録者

Liu, Y.,Tempel, W.,Dong, A.,Loppnau, P.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2013-12-20, 公開日: 2014-03-26, 最終更新日: 2025-03-26)

主引用文献

Liu, Y.,Tempel, W.,Zhang, Q.,Liang, X.,Loppnau, P.,Qin, S.,Min, J.
Family-wide Characterization of Histone Binding Abilities of Human CW Domain-containing Proteins.
J.Biol.Chem., 291:9000-9013, 2016

PubMed Abstract: Covalent modifications of histone N-terminal tails play a critical role in regulating chromatin structure and controlling gene expression. These modifications are controlled by histone-modifying enzymes and read out by histone-binding proteins. Numerous proteins have been identified as histone modification readers. Here we report the family-wide characterization of histone binding abilities of human CW domain-containing proteins. We demonstrate that the CW domains in ZCWPW2 and MORC3/4 selectively recognize histone H3 trimethylated at Lys-4, similar to ZCWPW1 reported previously, while the MORC1/2 and LSD2 lack histone H3 Lys-4 binding ability. Our crystal structures of the CW domains of ZCWPW2 and MORC3 in complex with the histone H3 trimethylated at Lys-4 peptide reveal the molecular basis of this interaction. In each complex, two tryptophan residues in the CW domain form the "floor" and "right wall," respectively, of the methyllysine recognition cage. Our mutation results based on ZCWPW2 reveal that the right wall tryptophan residue is essential for binding, and the floor tryptophan residue enhances binding affinity. Our structural and mutational analysis highlights the conserved roles of the cage residues of CW domain across the histone methyllysine binders but also suggests why some CW domains lack histone binding ability.

PubMed: 26933034
DOI: 10.1074/jbc.M116.718973

実験手法

X-RAY DIFFRACTION (1.78 Å)