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1n72

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[[Image:1n72.png|left|200px]]
 
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==Structure and Ligand of a Histone Acetyltransferase Bromodomain==
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The line below this paragraph, containing "STRUCTURE_1n72", creates the "Structure Box" on the page.
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<StructureSection load='1n72' size='340' side='right'caption='[[1n72]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1n72]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b91 1b91]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N72 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n72 OCA], [https://pdbe.org/1n72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n72 RCSB], [https://www.ebi.ac.uk/pdbsum/1n72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n72 ProSAT]</span></td></tr>
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{{STRUCTURE_1n72| PDB=1n72 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n7/1n72_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1n72 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.
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===Structure and Ligand of a Histone Acetyltransferase Bromodomain===
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Structure and ligand of a histone acetyltransferase bromodomain.,Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM Nature. 1999 Jun 3;399(6735):491-6. PMID:10365964<ref>PMID:10365964</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1n72" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10365964}}, adds the Publication Abstract to the page
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10365964 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10365964}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1n72]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b91 1b91]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N72 OCA].
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==Reference==
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<ref group="xtra">PMID:010365964</ref><references group="xtra"/>
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[[Category: Histone acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aggarwal, A K.]]
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[[Category: Large Structures]]
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[[Category: Carlson, J E.]]
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[[Category: Aggarwal AK]]
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[[Category: Dhalluin, C.]]
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[[Category: Carlson JE]]
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[[Category: He, C.]]
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[[Category: Dhalluin C]]
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[[Category: Zeng, L.]]
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[[Category: He C]]
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[[Category: Zhou, M M.]]
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[[Category: Zeng L]]
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[[Category: 4-helical bundle]]
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[[Category: Zhou M-M]]
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[[Category: Histone acetyltransferase bromodomain]]
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Current revision

Structure and Ligand of a Histone Acetyltransferase Bromodomain

PDB ID 1n72

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