3s91: Difference between revisions

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New page: '''Unreleased structure''' The entry 3s91 is ON HOLD Authors: Filippakopoulos, P., Picaud, S., Qi, J., Keates, T., Felletar, I., Fedorov, O., Muniz, J., von Delft, F., Arrowsmith, C.H.,...
 
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'''Unreleased structure'''


The entry 3s91 is ON HOLD
==Crystal Structure of the first bromodomain of human BRD3 in complex with the inhibitor JQ1==
<StructureSection load='3s91' size='340' side='right'caption='[[3s91]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3s91]] 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=3S91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S91 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]] 2.06&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=JQ1:(6S)-6-(2-TERT-BUTOXY-2-OXOETHYL)-4-(4-CHLOROPHENYL)-2,3,9-TRIMETHYL-6,7-DIHYDROTHIENO[3,2-F][1,2,4]TRIAZOLO[4,3-A][1,4]DIAZEPIN-10-IUM'>JQ1</scene></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=3s91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s91 OCA], [https://pdbe.org/3s91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s91 RCSB], [https://www.ebi.ac.uk/pdbsum/3s91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s91 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/BRD3_HUMAN BRD3_HUMAN] Note=A chromosomal aberration involving BRD3 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;9)(q14;q34) with NUT which produces a BRD3-NUT fusion protein.
== Function ==
[https://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>


Authors: Filippakopoulos, P., Picaud, S., Qi, J., Keates, T., Felletar, I., Fedorov, O., Muniz, J., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Weigelt, J., Bountra, C., Bradner, J.E., Knapp, S., Structural Genomics Consortium (SGC)
==See Also==
 
*[[Bromodomain-containing protein 3D structures|Bromodomain-containing protein 3D structures]]
Description: Crystal Structure of the first bromodomain of human BRD3 in complex with the inhibitor JQ1
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Bradner JE]]
[[Category: Edwards AM]]
[[Category: Fedorov O]]
[[Category: Felletar I]]
[[Category: Filippakopoulos P]]
[[Category: Keates T]]
[[Category: Knapp S]]
[[Category: Muniz J]]
[[Category: Picaud S]]
[[Category: Qi J]]
[[Category: Weigelt J]]
[[Category: Von Delft F]]

Latest revision as of 15:50, 14 March 2024

Crystal Structure of the first bromodomain of human BRD3 in complex with the inhibitor JQ1Crystal Structure of the first bromodomain of human BRD3 in complex with the inhibitor JQ1

Structural highlights

3s91 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.06Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

BRD3_HUMAN Note=A chromosomal aberration involving BRD3 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;9)(q14;q34) with NUT which produces a BRD3-NUT fusion protein.

Function

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.[1]

See Also

References

  1. LeRoy G, Rickards B, Flint SJ. The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription. Mol Cell. 2008 Apr 11;30(1):51-60. doi: 10.1016/j.molcel.2008.01.018. PMID:18406326 doi:10.1016/j.molcel.2008.01.018

3s91, resolution 2.06Å

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