6G16
Structure of the human RBBP4:MTA1(464-546) complex showing loop exchange
Summary for 6G16
Entry DOI | 10.2210/pdb6g16/pdb |
EMDB information | 3399 |
Descriptor | Histone-binding protein RBBP4, Metastasis-associated protein MTA1 (2 entities in total) |
Functional Keywords | wd40, corepressor, metastasis, transcription |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 8 |
Total formula weight | 229932.34 |
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 citation | Millard, 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: 27098840DOI: 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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