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==Crystal structure of the bromodomain of human BRPF1B==
==Crystal structure of the bromodomain of human BRPF1B==
<StructureSection load='4lc2' size='340' side='right' caption='[[4lc2]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='4lc2' size='340' side='right'caption='[[4lc2]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lc2]] 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=4LC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LC2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lc2]] 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=4LC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LC2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.65&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BR140, BRPF1, BRPF1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=4lc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc2 OCA], [http://pdbe.org/4lc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4lc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lc2 ProSAT]</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=4lc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc2 OCA], [https://pdbe.org/4lc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lc2 RCSB], [https://www.ebi.ac.uk/pdbsum/4lc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lc2 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>
[https://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: Homo sapiens]]
[[Category: Arrowsmith, C H]]
[[Category: Large Structures]]
[[Category: Bountra, C]]
[[Category: Arrowsmith CH]]
[[Category: Delft, F von]]
[[Category: Bountra C]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Filippakopoulos, P]]
[[Category: Filippakopoulos P]]
[[Category: Knapp, S]]
[[Category: Knapp S]]
[[Category: Nunez-Alonso, G]]
[[Category: Nunez-Alonso G]]
[[Category: Picaud, S]]
[[Category: Picaud S]]
[[Category: Structural genomic]]
[[Category: Savitsky P]]
[[Category: Savitsky, P]]
[[Category: Tallant C]]
[[Category: Tallant, C]]
[[Category: Von Delft F]]
[[Category: Bromodomain and phd finger-containing protein 1]]
[[Category: Dna binding protein]]
[[Category: Protein br140]]
[[Category: Sgc]]

Latest revision as of 19:17, 20 September 2023

Crystal structure of the bromodomain of human BRPF1BCrystal structure of the bromodomain of human BRPF1B

Structural highlights

4lc2 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 1.65Å
Ligands:,
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

4lc2, resolution 1.65Å

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