6bgg
From Proteopedia
(Difference between revisions)
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<StructureSection load='6bgg' size='340' side='right' caption='[[6bgg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='6bgg' size='340' side='right' caption='[[6bgg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6bgg]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bgg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGG FirstGlance]. <br> |
| - | </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=6bgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgg OCA], [http://pdbe.org/6bgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgg RCSB], [http://www.ebi.ac.uk/pdbsum/6bgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgg ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRD3, KIAA0043, RING3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6bgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgg OCA], [http://pdbe.org/6bgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgg RCSB], [http://www.ebi.ac.uk/pdbsum/6bgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BRD3_HUMAN BRD3_HUMAN]] Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene.<ref>PMID:18406326</ref> | [[http://www.uniprot.org/uniprot/BRD3_HUMAN BRD3_HUMAN]] Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene.<ref>PMID:18406326</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Members of the bromodomain and extra-terminal domain (BET) family of proteins (bromodomain-containing (BRD) 2, 3, 4 and T) are widely expressed and highly conserved regulators of gene expression in eukaryotes. These proteins have been intimately linked to human disease and more than a dozen clinical trials are currently underway to test BET-protein inhibitors as modulators of cancer therapies. However, although it is clear that these proteins use their bromodomains to bind both histones and transcription factors bearing acetylated lysine residues, the molecular mechanisms by which BET-family proteins regulate gene expression are not well defined. In particular, the functions of the other domains such as the ET domain have been less extensively studied. Here, we examine the properties of the ET domain of BRD3 as a protein-protein interaction module. Using a combination of pulldown and biophysical assays, we demonstrate that BRD3 binds to a range of chromatin-remodeling complexes, including the NuRD, BAF and INO80 complexes, via a short linear 'KIKL' motif in one of the complex subunits. NMR-based structural analysis revealed that, surprisingly, this mode of interaction is shared by the AF9 and ENL transcriptional coregulators that contain an acetyllysine-binding YEATS domain and regulate transcriptional elongation. This observation establishes a functional commonality between these two families of cancer-related transcriptional regulators. In summary, our data provide insight into the mechanisms by which BET-family proteins might link chromatin acetylation to transcriptional outcomes and uncover an unexpected functional similarity between BET and YEATS family proteins. | ||
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| + | The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators.,Wai DC, Szyszka TN, Campbell AE, Kwong C, Wilkinson-White LE, Silva APG, Low JKK, Kwan AH, Gamsjaeger R, Chalmers JN, Patrick WM, Lu B, Vakoc CR, Blobel G, Mackay JP J Biol Chem. 2018 Mar 22. pii: RA117.000678. doi: 10.1074/jbc.RA117.000678. PMID:29567837<ref>PMID:29567837</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bgg" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Bromodomain-containing protein|Bromodomain-containing protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Blobel, G A]] | [[Category: Blobel, G A]] | ||
[[Category: Campbell, A E]] | [[Category: Campbell, A E]] | ||
Revision as of 06:55, 4 April 2018
Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide
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