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==Crystal structure of the bromodomain of human BRPF1 in complex with OF-1 chemical probe==
==Crystal structure of the bromodomain of human BRPF1 in complex with OF-1 chemical probe==
<StructureSection load='5fg4' size='340' side='right' caption='[[5fg4]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='5fg4' size='340' side='right'caption='[[5fg4]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fg4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FG4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5fg4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FG4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FG4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5XE:4-BROMANYL-~{N}-(6-METHOXY-1,3-DIMETHYL-2-OXIDANYLIDENE-BENZIMIDAZOL-5-YL)-2-METHYL-BENZENESULFONAMIDE'>5XE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5XE:4-BROMANYL-~{N}-(6-METHOXY-1,3-DIMETHYL-2-OXIDANYLIDENE-BENZIMIDAZOL-5-YL)-2-METHYL-BENZENESULFONAMIDE'>5XE</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=5fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fg4 OCA], [http://pdbe.org/5fg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/5fg4 PDBsum]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRPF1, BR140 ([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://proteopedia.org/fgij/fg.htm?mol=5fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fg4 OCA], [http://pdbe.org/5fg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/5fg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fg4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref>   
[[http://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref>   
==See Also==
*[[Peregrin|Peregrin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bountra, C]]

Revision as of 10:17, 6 May 2020

Crystal structure of the bromodomain of human BRPF1 in complex with OF-1 chemical probeCrystal structure of the bromodomain of human BRPF1 in complex with OF-1 chemical probe

Structural highlights

5fg4 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:BRPF1, BR140 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BRPF1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.[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. ↑ Ullah M, Pelletier N, Xiao L, Zhao SP, Wang K, Degerny C, Tahmasebi S, Cayrou C, Doyon Y, Goh SL, Champagne N, Cote J, Yang XJ. Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes. Mol Cell Biol. 2008 Nov;28(22):6828-43. doi: 10.1128/MCB.01297-08. Epub 2008 Sep , 15. PMID:18794358 doi:10.1128/MCB.01297-08

5fg4, resolution 1.65Å

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