6l87: Difference between revisions

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New page: '''Unreleased structure''' The entry 6l87 is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6l87 is ON HOLD
==Solution structure of the tandem PWWP-ARID domains of human RBBP1==
<StructureSection load='6l87' size='340' side='right'caption='[[6l87]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L87 FirstGlance]. <br>
</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=6l87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l87 OCA], [https://pdbe.org/6l87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l87 RCSB], [https://www.ebi.ac.uk/pdbsum/6l87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l87 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARI4A_HUMAN ARI4A_HUMAN] Interacts with the viral protein-binding domain of the retinoblastoma protein.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Retinoblastoma-binding protein 1 (RBBP1) is involved in gene regulation, epigenetic regulation, and disease processes. RBBP1 contains five domains with DNA-binding or histone-binding activities, but how RBBP1 specifically recognizes chromatin is still unknown. An AT-rich interaction domain (ARID) in RBBP1 was proposed to be the key region for DNA-binding and gene suppression. Here, we first determined the solution structure of a tandem PWWP-ARID domain mutant of RBBP1 after deletion of a long flexible acidic loop L12 in the ARID domain. NMR titration results indicated that the ARID domain interacts with DNA with no GC- or AT-rich preference. Surprisingly, we found that the loop L12 binds to the DNA-binding region of the ARID domain as a DNA mimic and inhibits DNA binding. The loop L12 can also bind weakly to the Tudor and chromobarrel domains of RBBP1, but binds more strongly to the DNA-binding region of the histone H2A-H2B heterodimer. Furthermore, both the loop L12 and DNA can enhance the binding of the chromobarrel domain to H3K4me3 and H4K20me3. Based on these results, we propose a model of chromatin recognition by RBBP1, which highlights the unexpected multiple key roles of the disordered acidic loop L12 in the specific binding of RBBP1 to chromatin.


Authors:  
Structural Insight into Chromatin Recognition by Multiple Domains of the Tumor Suppressor RBBP1.,Gong W, Liang Q, Tong Y, Perrett S, Feng Y J Mol Biol. 2021 Sep 8;433(21):167224. doi: 10.1016/j.jmb.2021.167224. PMID:34506790<ref>PMID:34506790</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6l87" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Feng YG]]
[[Category: Gong WB]]
[[Category: Perrett S]]

Latest revision as of 10:53, 14 June 2023

Solution structure of the tandem PWWP-ARID domains of human RBBP1

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