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6e83
From Proteopedia
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<StructureSection load='6e83' size='340' side='right' caption='[[6e83]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='6e83' size='340' side='right' caption='[[6e83]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6e83]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E83 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E83 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZZZ3 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e83 OCA], [http://pdbe.org/6e83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e83 RCSB], [http://www.ebi.ac.uk/pdbsum/6e83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e83 ProSAT]</span></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=6e83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e83 OCA], [http://pdbe.org/6e83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e83 RCSB], [http://www.ebi.ac.uk/pdbsum/6e83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e83 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ZZZ3_HUMAN ZZZ3_HUMAN]] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.<ref>PMID:19103755</ref> | [[http://www.uniprot.org/uniprot/ZZZ3_HUMAN ZZZ3_HUMAN]] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.<ref>PMID:19103755</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recognition of histones by epigenetic readers is a fundamental mechanism for the regulation of chromatin and transcription. Most reader modules target specific post-translational modifications on histones. Here, we report the identification of a reader of histone H3, the ZZ-type zinc finger (ZZ) domain of ZZZ3, a subunit of the Ada-two-A-containing (ATAC) histone acetyltransferase complex. The solution NMR structure of the ZZ in complex with the H3 peptide reveals a unique binding mechanism involving caging of the N-terminal Alanine 1 of histone H3 in an acidic cavity of the ZZ domain, indicating a specific recognition of H3 versus other histones. Depletion of ZZZ3 or disruption of the ZZ-H3 interaction dampens ATAC-dependent promoter histone H3K9 acetylation and target gene expression. Overall, our study identifies the ZZ domain of ZZZ3 as a histone H3 reader that is required for the ATAC complex-mediated maintenance of histone acetylation and gene activation. | ||
| + | |||
| + | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation.,Mi W, Zhang Y, Lyu J, Wang X, Tong Q, Peng D, Xue Y, Tencer AH, Wen H, Li W, Kutateladze TG, Shi X Nat Commun. 2018 Sep 14;9(1):3759. doi: 10.1038/s41467-018-06247-5. PMID:30217978<ref>PMID:30217978</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6e83" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Kutateladze, T G]] | [[Category: Kutateladze, T G]] | ||
[[Category: Zhang, Y]] | [[Category: Zhang, Y]] | ||
Revision as of 08:48, 3 October 2018
Solution structure of ZZZ3 ZZ domain in complex with histone H3 tail
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Categories: Human | Kutateladze, T G | Zhang, Y | Chromatin | Gene regulation | Histone | Zz domain | Zzz3
