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3uvw

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Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H4K5acK8ac)

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 ==Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H4K5acK8ac)==
-<StructureSection load='3uvw' size='340' side='right' caption='[[3uvw]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
+<StructureSection load='3uvw' size='340' side='right'caption='[[3uvw]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uvw]] is a 2 chain structure 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=3UVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UVW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uvw]] 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=3UVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uv2|3uv2]], [[3uv4|3uv4]], [[3uv5|3uv5]], [[3uvd|3uvd]], [[3uvx|3uvx]], [[3uvy|3uvy]], [[3uw9|3uw9]]</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=3uvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvw OCA], [https://pdbe.org/3uvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvw RCSB], [https://www.ebi.ac.uk/pdbsum/3uvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvw ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRD4, HUNK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uvw RCSB], [http://www.ebi.ac.uk/pdbsum/3uvw PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN]] Note=A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein.<ref>PMID:12543779</ref> <ref>PMID:11733348</ref>
+[https://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN] Note=A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein.<ref>PMID:12543779</ref> <ref>PMID:11733348</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN]] Plays a role in a process governing chromosomal dynamics during mitosis (By similarity).
+[https://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN] Plays a role in a process governing chromosomal dynamics during mitosis (By similarity).
-<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Bromodomain-containing protein 3D structures|Bromodomain-containing protein 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 20: @@
 </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: Felletar, I]]
+[[Category: Felletar I]]
-[[Category: Filippakopoulos, P]]
+[[Category: Filippakopoulos P]]
-[[Category: Gileadi, O]]
+[[Category: Gileadi O]]
-[[Category: Keates, T]]
+[[Category: Keates T]]
-[[Category: Knapp, S]]
+[[Category: Knapp S]]
-[[Category: Muniz, J]]
+[[Category: Muniz J]]
-[[Category: Picaud, S]]
+[[Category: Picaud S]]
-[[Category: Structural genomic]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J]]
+[[Category: Von Delft F]]
-[[Category: Bromodomain]]
-[[Category: Bromodomain containing protein 4]]
-[[Category: Cap]]
-[[Category: Hunk1]]
-[[Category: Mcap]]
-[[Category: Mitotic chromosome associated protein]]
-[[Category: Peptide complex]]
-[[Category: Protein binding]]
-[[Category: Sgc]]
-[[Category: Transcription]]
-[[Category: Transcription-protein binding complex]]

3uvw

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Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H4K5acK8ac)

Structural highlights

Disease

Function

See Also

References

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