2xu7: Difference between revisions
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< | ==Structural basis for RbAp48 binding to FOG-1== | ||
<StructureSection load='2xu7' size='340' side='right'caption='[[2xu7]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xu7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XU7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xu7 OCA], [https://pdbe.org/2xu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2xu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xu7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RBBP4_HUMAN 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.<ref>PMID:10866654</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chromatin modifying complexes such as the NuRD complex are recruited to particular genomic sites by gene-specific nuclear factors. Overall, however, little is known about the molecular basis for these interactions. Here we present the 1.9-Angstrom resolution crystal structure of the NuRD subunit RbAp48 bound to the 15 N-terminal amino acids of the GATA-1 cofactor FOG-1. The FOG-1 peptide contacts a negatively charged binding pocket on top of the RbAp48 beta-propeller that is distinct from the binding surface used by RpAp48 to contact histone H4. We further show that RbAp48 interacts with the NuRD subunit Metastasis Associated-1 (MTA-1) via a surface that is distinct from its FOG-binding pocket, providing a first glimpse into the way in which NuRD assembly facilitates interactions with cofactors. Our RbAp48-FOG structure provides insight into the molecular determinants of FOG-1 dependent association with the NuRD complex and into the links between transcriptional regulation and nucleosome remodelling. | |||
Insights into the association of the nucleosome remodelling and deacetylase (NURD) complex with friend of gata-1 (FOG-1) from the crystal structure of a retinoblastoma associated protein-48 (RBAP48) fog-1 complex.,Lejon S, Thong SY, Murthy A, Alqarni S, Murzina NV, Blobel GA, Laue ED, Mackay JP J Biol Chem. 2010 Nov 2. PMID:21047798<ref>PMID:21047798</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xu7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Blobel | [[Category: Large Structures]] | ||
[[Category: Laue | [[Category: Blobel GA]] | ||
[[Category: Lejon | [[Category: Laue ED]] | ||
[[Category: Mackay | [[Category: Lejon S]] | ||
[[Category: Murthy | [[Category: Mackay JP]] | ||
[[Category: Murzina | [[Category: Murthy A]] | ||
[[Category: Thong | [[Category: Murzina NV]] | ||
[[Category: Thong SY]] | |||
Latest revision as of 13:39, 20 December 2023
Structural basis for RbAp48 binding to FOG-1Structural basis for RbAp48 binding to FOG-1
Structural highlights
FunctionRBBP4_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] Publication Abstract from PubMedChromatin modifying complexes such as the NuRD complex are recruited to particular genomic sites by gene-specific nuclear factors. Overall, however, little is known about the molecular basis for these interactions. Here we present the 1.9-Angstrom resolution crystal structure of the NuRD subunit RbAp48 bound to the 15 N-terminal amino acids of the GATA-1 cofactor FOG-1. The FOG-1 peptide contacts a negatively charged binding pocket on top of the RbAp48 beta-propeller that is distinct from the binding surface used by RpAp48 to contact histone H4. We further show that RbAp48 interacts with the NuRD subunit Metastasis Associated-1 (MTA-1) via a surface that is distinct from its FOG-binding pocket, providing a first glimpse into the way in which NuRD assembly facilitates interactions with cofactors. Our RbAp48-FOG structure provides insight into the molecular determinants of FOG-1 dependent association with the NuRD complex and into the links between transcriptional regulation and nucleosome remodelling. Insights into the association of the nucleosome remodelling and deacetylase (NURD) complex with friend of gata-1 (FOG-1) from the crystal structure of a retinoblastoma associated protein-48 (RBAP48) fog-1 complex.,Lejon S, Thong SY, Murthy A, Alqarni S, Murzina NV, Blobel GA, Laue ED, Mackay JP J Biol Chem. 2010 Nov 2. PMID:21047798[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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