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5fxy

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Revision as of 07:42, 6 May 2020

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

Structural highlights

5fxy is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBBP4_HUMAN] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.^[1] [MTA1_HUMAN] May be involved in the regulation of gene expression by covalent modification of histone proteins. Isoform Long is a corepressor of estrogen receptor (ER). Isoform Short binds to ER and sequesters it in the cytoplasm and enhances non-genomic responses of ER.

Publication Abstract from PubMed

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.

The structure of the core NuRD repression complex provides insights into its interaction with chromatin.,Millard CJ, Varma N, Saleh A, Morris K, Watson PJ, Bottrill AR, Fairall L, Smith CJ, Schwabe JW Elife. 2016 Apr 21;5. pii: e13941. doi: 10.7554/eLife.13941. PMID:27098840^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhang Q, Vo N, Goodman RH. Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. Mol Cell Biol. 2000 Jul;20(14):4970-8. PMID:10866654
↑ Millard CJ, Varma N, Saleh A, Morris K, Watson PJ, Bottrill AR, Fairall L, Smith CJ, Schwabe JW. The structure of the core NuRD repression complex provides insights into its interaction with chromatin. Elife. 2016 Apr 21;5. pii: e13941. doi: 10.7554/eLife.13941. PMID:27098840 doi:http://dx.doi.org/10.7554/eLife.13941

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fxy"

@@ Line 1: / Line 1: @@
 ==Structure of the human RBBP4:MTA1(464-546) complex==
-<StructureSection load='5fxy' size='340' side='right' caption='[[5fxy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='5fxy' size='340' side='right'caption='[[5fxy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fxy]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FXY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fxy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FXY FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxy OCA], [http://pdbe.org/5fxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fxy RCSB], [http://www.ebi.ac.uk/pdbsum/5fxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxy ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxy OCA], [http://pdbe.org/5fxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fxy RCSB], [http://www.ebi.ac.uk/pdbsum/5fxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxy ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 ==See Also==
-*[[Retinoblastoma-binding protein|Retinoblastoma-binding protein]]
+*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Fairall, L]]
 [[Category: Millard, C J]]

5fxy

From Proteopedia

Revision as of 07:42, 6 May 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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