5ffw: Difference between revisions

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==Crystal structure of the bromodomain of human BRPF1 in complex with H4K5acK8ac histone peptide==
==Crystal structure of the bromodomain of human BRPF1 in complex with H4K5acK8ac histone peptide==
<StructureSection load='5ffw' size='340' side='right' caption='[[5ffw]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='5ffw' size='340' side='right'caption='[[5ffw]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ffw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FFW FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ffw]] is a 3 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=5FFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FFW FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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]] 1.5&#8491;</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=5ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffw OCA], [http://pdbe.org/5ffw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ffw RCSB], [http://www.ebi.ac.uk/pdbsum/5ffw PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=5ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffw OCA], [https://pdbe.org/5ffw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ffw RCSB], [https://www.ebi.ac.uk/pdbsum/5ffw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffw 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/Q0VAS5_HUMAN Q0VAS5_HUMAN]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[RuleBase:RU000528]  Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).[SAAS:SAAS00349935]  
[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: Arrowsmith, C H]]
[[Category: Homo sapiens]]
[[Category: Bountra, C]]
[[Category: Large Structures]]
[[Category: Delft, F von]]
[[Category: Arrowsmith CH]]
[[Category: Edwards, A M]]
[[Category: Bountra C]]
[[Category: Knapp, S]]
[[Category: Edwards AM]]
[[Category: Krojer, T]]
[[Category: Knapp S]]
[[Category: Nunez-Alonso, G]]
[[Category: Krojer T]]
[[Category: Savitsky, P]]
[[Category: Nunez-Alonso G]]
[[Category: Tallant, C]]
[[Category: Savitsky P]]
[[Category: Moz-morf complex]]
[[Category: Tallant C]]
[[Category: Peregrin]]
[[Category: Von Delft F]]
[[Category: Transcription]]

Latest revision as of 11:53, 23 October 2024

Crystal structure of the bromodomain of human BRPF1 in complex with H4K5acK8ac histone peptideCrystal structure of the bromodomain of human BRPF1 in complex with H4K5acK8ac histone peptide

Structural highlights

5ffw is a 3 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 1.5Å
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

5ffw, resolution 1.50Å

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