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6G16

Structure of the human RBBP4:MTA1(464-546) complex showing loop exchange

Summary for 6G16
Entry DOI10.2210/pdb6g16/pdb
EMDB information3399
DescriptorHistone-binding protein RBBP4, Metastasis-associated protein MTA1 (2 entities in total)
Functional Keywordswd40, corepressor, metastasis, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains8
Total formula weight229932.34
Authors
Millard, C.J.,Varma, N.,Fairall, L.,Schwabe, J.W.R. (deposition date: 2018-03-20, release date: 2018-06-13, Last modification date: 2024-01-17)
Primary citationMillard, C.J.,Varma, N.,Saleh, A.,Morris, K.,Watson, P.J.,Bottrill, A.R.,Fairall, L.,Smith, C.J.,Schwabe, J.W.
The structure of the core NuRD repression complex provides insights into its interaction with chromatin.
Elife, 5:e13941-e13941, 2016
Cited by
PubMed Abstract: The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities. The complex regulates the higher-order structure of chromatin, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation. HDACs 1 and 2 are recruited by the MTA1 corepressor to form the catalytic core of the complex. The histone chaperone protein RBBP4, has previously been shown to bind to the carboxy-terminal tail of MTA1. We show that MTA1 recruits a second copy of RBBP4. The crystal structure reveals an extensive interface between MTA1 and RBBP4. An EM structure, supported by SAXS and crosslinking, reveals the architecture of the dimeric HDAC1:MTA1:RBBP4 assembly which forms the core of the NuRD complex. We find evidence that in this complex RBBP4 mediates interaction with histone H3 tails, but not histone H4, suggesting a mechanism for recruitment of the NuRD complex to chromatin.
PubMed: 27098840
DOI: 10.7554/eLife.13941
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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数据于2025-07-02公开中

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