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4nsq
From Proteopedia
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==Crystal structure of PCAF== | ==Crystal structure of PCAF== | ||
| - | <StructureSection load='4nsq' size='340' side='right' caption='[[4nsq]], [[Resolution|resolution]] 2.31Å' scene=''> | + | <StructureSection load='4nsq' size='340' side='right'caption='[[4nsq]], [[Resolution|resolution]] 2.31Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4nsq]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4nsq]] is a 4 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=4NSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NSQ FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3108Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nsq OCA], [https://pdbe.org/4nsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nsq RCSB], [https://www.ebi.ac.uk/pdbsum/4nsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nsq ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref> | |
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| - | + | ==See Also== | |
| - | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] | |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Cai | + | [[Category: Cai YF]] |
| - | [[Category: Lin | + | [[Category: Lin JY]] |
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Current revision
Crystal structure of PCAF
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