4PBY

Structure of the human RbAp48-MTA1(656-686) complex

4PBY の概要

• エントリーDOI: 10.2210/pdb4pby/pdb
• 分子名称: Histone-binding protein RBBP4, Metastasis-associated protein MTA1, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: rbap48, mta1, nurd, sub-complex, cell cycle
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: Q09028; Isoform Short: Cytoplasm. Isoform Long: Nucleus: Q13330
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102961.84

構造登録者

Murthy, A.,Lejon, S.,Alqarni, S.S.M.,Silva, A.P.G.,Watson, A.A.,Mackay, J.P.,Laue, E.D. (登録日: 2014-04-14, 公開日: 2014-06-11, 最終更新日: 2024-05-01)

主引用文献

Alqarni, S.S.,Murthy, A.,Zhang, W.,Przewloka, M.R.,Silva, A.P.,Watson, A.A.,Lejon, S.,Pei, X.Y.,Smits, A.H.,Kloet, S.L.,Wang, H.,Shepherd, N.E.,Stokes, P.H.,Blobel, G.A.,Vermeulen, M.,Glover, D.M.,Mackay, J.P.,Laue, E.D.
Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 sub-complex.
J.Biol.Chem., 289:21844-, 2014

PubMed Abstract: The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRD by determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.

PubMed: 24920672
DOI: 10.1074/jbc.M114.558940

実験手法

X-RAY DIFFRACTION (2.5 Å)