5ffw

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<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 ==
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<table><tr><td colspan='2'>[[5ffw]] is a 3 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=5FFW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FFW FirstGlance]. <br>
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<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>
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</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>
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</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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffw ProSAT]</span></td></tr>
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<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 ==
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[[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]
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[https://www.uniprot.org/uniprot/H4_HUMAN H4_HUMAN]
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==See Also==
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*[[Peregrin|Peregrin]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Nunez-Alonso G]]
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[[Category: Nunez-Alonso, G]]
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[[Category: Savitsky P]]
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[[Category: Savitsky, P]]
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[[Category: Tallant C]]
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[[Category: Tallant, C]]
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[[Category: Von Delft F]]
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[[Category: Moz-morf complex]]
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[[Category: Peregrin]]
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[[Category: Transcription]]
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Revision as of 06:49, 19 July 2023

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

PDB ID 5ffw

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