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4PC0

Structure of the human RbAp48-MTA1(670-711) complex

Summary for 4PC0
Entry DOI10.2210/pdb4pc0/pdb
Related4PBY 4PBZ
DescriptorHistone-binding protein RBBP4, Metastasis-associated protein MTA1, GLYCEROL, ... (5 entities in total)
Functional Keywordscell cycle, mta1-nurd subcomplex
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus: Q09028
Isoform Short: Cytoplasm. Isoform Long: Nucleus: Q13330
Total number of polymer chains4
Total formula weight104896.11
Authors
Alqarni, S.S.M.,Silva, A.P.G.,Mackay, J.P.,Laue, E.D. (deposition date: 2014-04-14, release date: 2014-06-11, Last modification date: 2023-12-20)
Primary citationAlqarni, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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