2ktb: Difference between revisions

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[[Image:2ktb.png|left|200px]]


{{STRUCTURE_2ktb| PDB=2ktb | SCENE= }}
==Solution Structure of the Second Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3==
<StructureSection load='2ktb' size='340' side='right'caption='[[2ktb]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ktb]] is a 2 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=2KTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KTB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=2ktb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktb OCA], [https://pdbe.org/2ktb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ktb RCSB], [https://www.ebi.ac.uk/pdbsum/2ktb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ktb ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PB1_HUMAN PB1_HUMAN] Defects in PBRM1 are a cause of renal cell carcinoma (RCC) [MIM:[https://omim.org/entry/144700 144700]. It is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma.<ref>PMID:21248752</ref>
== Function ==
[https://www.uniprot.org/uniprot/PB1_HUMAN PB1_HUMAN] Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation.<ref>PMID:21248752</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kt/2ktb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ktb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Polybromo (PB) protein functions as a key component of the human PBAF chromatin remodeling complex in regulation of gene transcription. PB is made up of modular domains including six bromodomains that are known as acetyl-lysine binding domains. However, histone-binding specificity of the bromodomains of PB has remained elusive. In this study, we report biochemical characterization of all six PB bromodomains' binding to a suite of lysine-acetylated peptides derived from known acetylation sites on human core histones. We demonstrate that bromodomain 2 of PB preferentially recognizes acetylated lysine 14 of histone H3 (H3K14ac), a post-translational mark known for gene transcriptional activation. We further describe the molecular basis of the selective H3K14ac recognition of bromodomain 2 by solving the protein structures in both the free and bound forms using X-ray crystallography and NMR, respectively.


===Solution Structure of the Second Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3===
Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2.,Charlop-Powers Z, Zeng L, Zhang Q, Zhou MM Cell Res. 2010 May;20(5):529-38. Epub 2010 Apr 6. PMID:20368734<ref>PMID:20368734</ref>


{{ABSTRACT_PUBMED_20368734}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2ktb" style="background-color:#fffaf0;"></div>
[[2ktb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTB OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:020368734</ref><references group="xtra"/>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Charlop-Powers, Z.]]
[[Category: Large Structures]]
[[Category: Zeng, L.]]
[[Category: Charlop-Powers Z]]
[[Category: Zhang, Q.]]
[[Category: Zeng L]]
[[Category: Bromodomain]]
[[Category: Zhang Q]]
[[Category: Chromatin regulator]]
[[Category: Dna-binding]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protein binding]]
[[Category: Transcription]]
[[Category: Transcription regulation]]

Latest revision as of 09:15, 6 November 2024

Solution Structure of the Second Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3

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