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| <StructureSection load='6zfg' size='340' side='right'caption='[[6zfg]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='6zfg' size='340' side='right'caption='[[6zfg]], [[Resolution|resolution]] 1.85Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6zfg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZFG FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZFG FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FSC:FUSICOCCIN'>FSC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FSC:FUSICOCCIN'>FSC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zfd|6zfd]]</div></td></tr>
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| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6zfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zfg OCA], [https://pdbe.org/6zfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zfg RCSB], [https://www.ebi.ac.uk/pdbsum/6zfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zfg ProSAT]</span></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=6zfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zfg OCA], [https://pdbe.org/6zfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zfg RCSB], [https://www.ebi.ac.uk/pdbsum/6zfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zfg ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
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| [[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The seven 14-3-3 isoforms are highly abundant human proteins encoded by similar yet distinct genes. 14-3-3 proteins recognize phosphorylated motifs within numerous human and viral proteins. Here, we analyze by X-ray crystallography, fluorescence polarization, mutagenesis and fusicoccin-mediated modulation the structural basis and druggability of 14-3-3 binding to four E6 oncoproteins of tumorigenic human papillomaviruses. 14-3-3 isoforms bind variant and mutated phospho-motifs of E6 and unrelated protein RSK1 with different affinities, albeit following an ordered affinity ranking with conserved relative KD ratios. Remarkably, 14-3-3 isoforms obey the same hierarchy when binding to most of their established targets, as supported by literature and a recent human complexome map. This knowledge allows predicting proportions of 14-3-3 isoforms engaged with phosphoproteins in various tissues. Notwithstanding their individual functions, cellular concentrations of 14-3-3 may be collectively adjusted to buffer the strongest phosphorylation outbursts, explaining their expression variations in different tissues and tumors.
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| Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms.,Gogl G, Tugaeva KV, Eberling P, Kostmann C, Trave G, Sluchanko NN Nat Commun. 2021 Mar 15;12(1):1677. doi: 10.1038/s41467-021-21908-8. PMID:33723253<ref>PMID:33723253</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6zfg" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Gogl, G]] | | [[Category: Gogl G]] |
| [[Category: Sluchanko, N N]] | | [[Category: Sluchanko NN]] |
| [[Category: Trave, G]] | | [[Category: Trave G]] |
| [[Category: Tugaeva, K]] | | [[Category: Tugaeva K]] |
| [[Category: 14-3-3]]
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| [[Category: E6 oncoprotein]]
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| [[Category: Hpv]]
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| [[Category: Protein binding]]
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