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==Solution structure of BRD1 PHD1 finger==
==Solution structure of BRD1 PHD1 finger==
<StructureSection load='2ku3' size='340' side='right' caption='[[2ku3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2ku3' size='340' side='right' caption='[[2ku3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRD1 ([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=2ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku3 OCA], [http://pdbe.org/2ku3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku3 PDBsum]</span></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=2ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku3 OCA], [http://pdbe.org/2ku3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku3 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>   
[[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>   
==See Also==
*[[Bromodomain-containing protein|Bromodomain-containing protein]]
== References ==
== References ==
<references/>
<references/>

Revision as of 11:25, 25 July 2018

Solution structure of BRD1 PHD1 fingerSolution structure of BRD1 PHD1 finger

Structural highlights

2ku3 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:BRD1 (HUMAN)
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
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