5ame: Difference between revisions

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New page: ==Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)==...
 
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==Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)==
==Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)==
<StructureSection load='5ame' size='340' side='right' caption='[[5ame]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='5ame' size='340' side='right'caption='[[5ame]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ame]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AME FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ame]] 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=5AME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AME FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PW3:4-ACETYL-PIPERAZIN-2-ONE'>PW3</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]] 1.578&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5amf|5amf]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PW3:4-ACETYL-PIPERAZIN-2-ONE'>PW3</scene></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=5ame FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ame OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ame RCSB], [http://www.ebi.ac.uk/pdbsum/5ame PDBsum]</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=5ame FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ame OCA], [https://pdbe.org/5ame PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ame RCSB], [https://www.ebi.ac.uk/pdbsum/5ame PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ame ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref>
[https://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref>  
 
==See Also==
*[[Bromodomain-containing protein 3D structures|Bromodomain-containing protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arrowsmith, C H]]
[[Category: Homo sapiens]]
[[Category: Bountra, C]]
[[Category: Large Structures]]
[[Category: Bowkett, D]]
[[Category: Arrowsmith CH]]
[[Category: Bradley, A]]
[[Category: Bountra C]]
[[Category: Brandao-Neto, J]]
[[Category: Bowkett D]]
[[Category: Brennan, P]]
[[Category: Bradley A]]
[[Category: Burgess-Brown, N]]
[[Category: Brandao-Neto J]]
[[Category: Collins, P]]
[[Category: Brennan P]]
[[Category: Cox, O]]
[[Category: Burgess-Brown N]]
[[Category: Delft, F von]]
[[Category: Collins P]]
[[Category: Douangamath, A]]
[[Category: Cox O]]
[[Category: Edwards, E]]
[[Category: Douangamath A]]
[[Category: Fairhead, M]]
[[Category: Edwards E]]
[[Category: Krojer, T]]
[[Category: Fairhead M]]
[[Category: Ng, J T]]
[[Category: Krojer T]]
[[Category: Pearce, N M]]
[[Category: Ng JT]]
[[Category: Strain-Damerell, C]]
[[Category: Pearce NM]]
[[Category: Talon, R]]
[[Category: Strain-Damerell C]]
[[Category: Wright, N]]
[[Category: Talon R]]
[[Category: Bromodomain]]
[[Category: Wright N]]
[[Category: Diamond i04-1]]
[[Category: Von Delft F]]
[[Category: Epigenetic]]
[[Category: Fragmentscreening]]
[[Category: Histone-binding protein]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Transcription]]

Latest revision as of 10:21, 1 May 2024

Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)

Structural highlights

5ame is a 2 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 1.578Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BRD1_HUMAN Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.[1] [2]

See Also

References

  1. ↑ Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007
  2. ↑ Qin S, Jin L, Zhang J, Liu L, Ji P, Wu M, Wu J, Shi Y. Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF). J Biol Chem. 2011 Oct 21;286(42):36944-55. doi: 10.1074/jbc.M111.244400. Epub, 2011 Aug 31. PMID:21880731 doi:http://dx.doi.org/10.1074/jbc.M111.244400

5ame, resolution 1.58Å

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