3uv2

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Current revision (14:08, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3uv2' size='340' side='right'caption='[[3uv2]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='3uv2' size='340' side='right'caption='[[3uv2]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3uv2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UV2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3uv2]] is a 1 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=3UV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UV2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7PE:2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL'>7PE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uv4|3uv4]], [[3uv5|3uv5]], [[3uvd|3uvd]], [[3uvw|3uvw]], [[3uvx|3uvx]], [[3uvy|3uvy]], [[3uw9|3uw9]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7PE:2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL'>7PE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BPTF, FAC1, FALZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3uv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uv2 OCA], [https://pdbe.org/3uv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uv2 RCSB], [https://www.ebi.ac.uk/pdbsum/3uv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uv2 ProSAT]</span></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=3uv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uv2 OCA], [https://pdbe.org/3uv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uv2 RCSB], [https://www.ebi.ac.uk/pdbsum/3uv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uv2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/BPTF_HUMAN BPTF_HUMAN]] Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors.
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[https://www.uniprot.org/uniprot/BPTF_HUMAN BPTF_HUMAN] Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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 3uv2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Filippakopoulos P]]
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[[Category: Filippakopoulos, P]]
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[[Category: Keates T]]
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[[Category: Keates, T]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Picaud S]]
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[[Category: Picaud, S]]
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[[Category: Ugochukwu E]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Ugochukwu, E]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J]]
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[[Category: Bptf]]
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[[Category: Bromodomain]]
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[[Category: Bromodomain and phd finger-containing transcription factor]]
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[[Category: Fac1]]
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[[Category: Falz]]
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[[Category: Fetal alz-50 clone 1 protein]]
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[[Category: Fetal alzheimer antigen]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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Current revision

Crystal structure of the bromodomain of human nucleosome-remodeling factor subunit BPTF

PDB ID 3uv2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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