2GNQ

Structure of wdr5

2GNQ の概要

• エントリーDOI: 10.2210/pdb2gnq/pdb
• 分子名称: WD-repeat protein 5, CHLORIDE ION (3 entities in total)
• 機能のキーワード: h3k4me2 binding protein, structural genomics, structural genomics consortium, sgc, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P61964
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36815.02

構造登録者

Min, J.,Schuetz, A.,Allali-Hassani, A.,Loppnau, P.,Vedadi, M.,Weigelt, J.,Sundstrom, M.,Edwards, A.M.,Arrowsmith, C.H.,Bochkarev, A.,Plotnikov, A.N.,Structural Genomics Consortium (SGC) (登録日: 2006-04-10, 公開日: 2006-06-06, 最終更新日: 2023-08-30)

主引用文献

Schuetz, A.,Allali-Hassani, A.,Loppnau, P.,Vedadi, M.,Bochkarev, A.,Plotnikov, A.N.,Arrowsmith, C.H.,Min, J.
Structural basis for molecular recognition and presentation of histone H3 By WDR5.
Embo J., 25:4245-4252, 2006

PubMed Abstract: Histone methylation at specific lysine residues brings about various downstream events that are mediated by different effector proteins. The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here we report the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. The structures reveal that WDR5 is able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified lysine 4. We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes.

PubMed: 16946699
DOI: 10.1038/sj.emboj.7601316

実験手法

X-RAY DIFFRACTION (1.8 Å)