3gg3: Difference between revisions

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-[[Image:3gg3.png|left|200px]]
-<!--
+==Crystal Structure of the Bromodomain of Human PCAF==
-The line below this paragraph, containing "STRUCTURE_3gg3", creates the "Structure Box" on the page.
+<StructureSection load='3gg3' size='340' side='right'caption='[[3gg3]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3gg3]] is a 2 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=3GG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GG3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-{{STRUCTURE_3gg3|  PDB=3gg3  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gg3 OCA], [https://pdbe.org/3gg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gg3 RCSB], [https://www.ebi.ac.uk/pdbsum/3gg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gg3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/gg/3gg3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3gg3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bromodomains (BRDs) are protein interaction modules that specifically recognize epsilon-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present 29 high-resolution crystal structures, covering all BRD families. Comprehensive crossfamily structural analysis identifies conserved and family-specific structural features that are necessary for specific acetylation-dependent substrate recognition. Screening of more than 30 representative BRDs against systematic histone-peptide arrays identifies new BRD substrates and reveals a strong influence of flanking posttranslational modifications, such as acetylation and phosphorylation, suggesting that BRDs recognize combinations of marks rather than singly acetylated sequences. We further uncovered a structural mechanism for the simultaneous binding and recognition of diverse diacetyl-containing peptides by BRD4. These data provide a foundation for structure-based drug design of specific inhibitors for this emerging target family.
-===Crystal Structure of the Bromodomain of Human PCAF===
+Histone recognition and large-scale structural analysis of the human bromodomain family.,Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S Cell. 2012 Mar 30;149(1):214-31. PMID:22464331<ref>PMID:22464331</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_22464331}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3gg3" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 22464331 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_22464331}}
-==About this Structure==
-[[3gg3]] is a 2 chain structure of [[Histone acetyltransferase]] 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=3GG3 OCA].
 ==See Also==
-*[[Histone acetyltransferase|Histone acetyltransferase]]
+*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:022464331</ref><references group="xtra"/>
+__TOC__
-[[Category: Histone acetyltransferase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Large Structures]]
-[[Category: Bountra, C.]]
+[[Category: Arrowsmith CH]]
-[[Category: Delft, F Von.]]
+[[Category: Bountra C]]
-[[Category: Edwards, A M.]]
+[[Category: Edwards AM]]
-[[Category: Fedorov, O.]]
+[[Category: Fedorov O]]
-[[Category: Filippakopoulos, P.]]
+[[Category: Filippakopoulos P]]
-[[Category: Keates, T.]]
+[[Category: Keates T]]
-[[Category: Knapp, S.]]
+[[Category: Knapp S]]
-[[Category: Picaud, S.]]
+[[Category: Picaud S]]
-[[Category: Rehana, K.]]
+[[Category: Rehana K]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Ugochukwu E]]
-[[Category: Ugochukwu, E.]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J.]]
+[[Category: Von Delft F]]
-[[Category: Acyltransferase]]
-[[Category: Bromodomain]]
-[[Category: Cell cycle]]
-[[Category: Crebbp-associated factor]]
-[[Category: Gcn5]]
-[[Category: Gcn5l]]
-[[Category: Host-virus interaction]]
-[[Category: Kat2b]]
-[[Category: Nucleus]]
-[[Category: P/caf]]
-[[Category: P300/cbp-associated factor]]
-[[Category: Pcaf]]
-[[Category: Phosphoprotein]]
-[[Category: Sgc]]
-[[Category: Structural genomics consortium]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Transferase]]