5gk9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of human HBO1 in complex with BRPF2== | |
+ | <StructureSection load='5gk9' size='340' side='right'caption='[[5gk9]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5gk9]] is a 2 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=5GK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GK9 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5gk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk9 OCA], [https://pdbe.org/5gk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gk9 RCSB], [https://www.ebi.ac.uk/pdbsum/5gk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/KAT7_HUMAN KAT7_HUMAN] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1 (PubMed:18832067). Specifically represses AR-mediated transcription.<ref>PMID:10438470</ref> <ref>PMID:10930412</ref> <ref>PMID:11278932</ref> <ref>PMID:16387653</ref> <ref>PMID:18832067</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2. | ||
- | + | Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.,Tao Y, Zhong C, Zhu J, Xu S, Ding J Nucleic Acids Res. 2017 Jun 2;45(10):5707-5719. doi: 10.1093/nar/gkx142. PMID:28334966<ref>PMID:28334966</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Ding | + | <div class="pdbe-citations 5gk9" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: Xu | + | ==See Also== |
- | [[Category: | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Ding J]] | ||
+ | [[Category: Tao Y]] | ||
+ | [[Category: Xu S]] | ||
+ | [[Category: Zhu J]] |
Current revision
Crystal structure of human HBO1 in complex with BRPF2
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Categories: Homo sapiens | Large Structures | Ding J | Tao Y | Xu S | Zhu J