2L2L

Solution structure of the coiled-coil complex between MBD2 and p66alpha

2L2L の概要

• エントリーDOI: 10.2210/pdb2l2l/pdb
• NMR情報: BMRB: 17138
• 分子名称: Transcriptional repressor p66-alpha, Methyl-CpG-binding domain protein 2 (2 entities in total)
• 機能のキーワード: dna methylation, coiled-coil, nurd, mbd2, p66alpha, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9297.80

構造登録者

Williams Jr., D.C.,Scarsdale Jr., N. (登録日: 2010-08-20, 公開日: 2011-05-04, 最終更新日: 2024-05-01)

主引用文献

Gnanapragasam, M.N.,Scarsdale, J.N.,Amaya, M.L.,Webb, H.D.,Desai, M.A.,Walavalkar, N.M.,Wang, S.Z.,Zu Zhu, S.,Ginder, G.D.,Williams, D.C.
p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex.
Proc.Natl.Acad.Sci.USA, 108:7487-7492, 2011

PubMed Abstract: Nucleosome remodeling complexes comprise several large families of chromatin modifiers that integrate multiple epigenetic control signals to play key roles in cell type-specific transcription regulation. We previously isolated a methyl-binding domain protein 2 (MBD2)-containing nucleosome remodeling and deacetylation (NuRD) complex from primary erythroid cells and showed that MBD2 contributes to DNA methylation-dependent embryonic and fetal β-type globin gene silencing during development in vivo. Here we present structural and biophysical details of the coiled-coil interaction between MBD2 and p66α, a critical component of the MBD2-NuRD complex. We show that enforced expression of the isolated p66α coiled-coil domain relieves MBD2-mediated globin gene silencing and that the expressed peptide interacts only with a subset of components of the MBD2-NuRD complex that does not include native p66α or Mi-2. These results demonstrate the central importance of the coiled-coil interaction and suggest that MBD2-dependent DNA methylation-driven gene silencing can be disrupted by selectively targeting this coiled-coil complex.

PubMed: 21490301
DOI: 10.1073/pnas.1015341108

実験手法

SOLUTION NMR