3d7c
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:3d7c.png|left|200px]] | ||
- | + | ==Crystal structure of the bromodomain of human GCN5, the general control of amino-acid synthesis protein 5-like 2== | |
- | + | <StructureSection load='3d7c' size='340' side='right'caption='[[3d7c]], [[Resolution|resolution]] 2.06Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[3d7c]] 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=3D7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D7C FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06Å</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=3d7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d7c OCA], [https://pdbe.org/3d7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d7c RCSB], [https://www.ebi.ac.uk/pdbsum/3d7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d7c ProSAT]</span></td></tr> |
- | + | </table> | |
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/KAT2A_HUMAN KAT2A_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non-histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. 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:17301242</ref> <ref>PMID:19103755</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/d7/3d7c_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=3d7c 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. | ||
- | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 3d7c" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Arrowsmith CH]] |
- | [[Category: | + | [[Category: Bountra C]] |
- | [[Category: Edwards | + | [[Category: Edwards AM]] |
- | [[Category: Eswaran | + | [[Category: Eswaran J]] |
- | [[Category: Fedorov | + | [[Category: Fedorov O]] |
- | [[Category: Filippakopoulos | + | [[Category: Filippakopoulos P]] |
- | [[Category: Knapp | + | [[Category: Knapp S]] |
- | [[Category: Murray | + | [[Category: Murray J]] |
- | [[Category: Picaud | + | [[Category: Picaud S]] |
- | [[Category: | + | [[Category: Von Delft F]] |
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Current revision
Crystal structure of the bromodomain of human GCN5, the general control of amino-acid synthesis protein 5-like 2
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bountra C | Edwards AM | Eswaran J | Fedorov O | Filippakopoulos P | Knapp S | Murray J | Picaud S | Von Delft F