6ds6
From Proteopedia
(Difference between revisions)
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<StructureSection load='6ds6' size='340' side='right' caption='[[6ds6]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='6ds6' size='340' side='right' caption='[[6ds6]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6ds6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DS6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ds6]] 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=6DS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DS6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EP300, P300 ([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=6ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ds6 OCA], [http://pdbe.org/6ds6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ds6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ds6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ds6 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=6ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ds6 OCA], [http://pdbe.org/6ds6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ds6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ds6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ds6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Human p300 is a transcriptional co-activator and a major acetyltransferase that acetylates histones and other proteins facilitating gene transcription. The activity of p300 relies on the fine-tuned interactome that involves a dozen p300 domains and hundreds of binding partners and links p300 to a wide range of vital signaling events. Here, we report a novel function of the ZZ-type zinc finger (ZZ) of p300 as a reader of histone H3. We show that the ZZ domain and acetyllysine-recognizing bromodomain of p300 play critical roles in modulating p300 enzymatic activity and its association with chromatin. The acetyllysine binding function of bromodomain is essential for acetylation of histones H3 and H4, whereas interaction of the ZZ domain with H3 promotes selective acetylation of the histone H3K27 and H3K18 sites. | ||
+ | |||
+ | The ZZ domain of p300 mediates specificity of the adjacent HAT domain for histone H3.,Zhang Y, Xue Y, Shi J, Ahn J, Mi W, Ali M, Wang X, Klein BJ, Wen H, Li W, Shi X, Kutateladze TG Nat Struct Mol Biol. 2018 Sep;25(9):841-849. doi: 10.1038/s41594-018-0114-9. Epub, 2018 Aug 27. PMID:30150647<ref>PMID:30150647</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6ds6" style="background-color:#fffaf0;"></div> | ||
+ | == 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 07:52, 12 September 2018
Crystal structure of p300 ZZ domain in complex with histone H3 peptide
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Categories: Human | Kutateladze, T G | Zhang, Y | Chromatin | Gene regulation | Histone | P300 | Transferase | Zz domain