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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XU7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2xu7 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
==See Also== | ==See Also== | ||
*[[Retinoblastoma-binding protein|Retinoblastoma-binding protein]] | *[[Retinoblastoma-binding protein|Retinoblastoma-binding protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Blobel, G A.]] | [[Category: Blobel, G A.]] |