This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4pc0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:31, 11 August 2016

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

Structural highlights

4pc0 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4pby, 4pbz
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 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 ageing. We have investigated the architecture of NuRD by determining the structure of a sub-complex 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 shows 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.

Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 sub-complex.,Alqarni SS, Murthy A, Zhang W, Przewloka MR, Silva AP, Watson AA, Lejon S, Pei XY, Smits AH, Kloet SL, Wang H, Shepherd NE, Stokes PH, Blobel GA, Vermeulen M, Glover DM, Mackay JP, Laue ED J Biol Chem. 2014 Jun 11. pii: jbc.M114.558940. PMID:24920672^[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
↑ Alqarni SS, Murthy A, Zhang W, Przewloka MR, Silva AP, Watson AA, Lejon S, Pei XY, Smits AH, Kloet SL, Wang H, Shepherd NE, Stokes PH, Blobel GA, Vermeulen M, Glover DM, Mackay JP, Laue ED. Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 sub-complex. J Biol Chem. 2014 Jun 11. pii: jbc.M114.558940. PMID:24920672 doi:http://dx.doi.org/10.1074/jbc.M114.558940

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/4pc0"

@@ Line 1: / Line 1: @@
 ==Structure of the human RbAp48-MTA1(670-711) complex==
 <StructureSection load='4pc0' size='340' side='right' caption='[[4pc0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pby|4pby]], [[4pbz|4pbz]]</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=4pc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc0 PDBsum]</span></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=4pc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc0 OCA], [http://pdbe.org/4pc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pc0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4pc0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Retinoblastoma-binding protein|Retinoblastoma-binding protein]]
 == References ==
 <references/>

4pc0

From Proteopedia

Revision as of 08:31, 11 August 2016

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox