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==The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide==
==The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide==
<StructureSection load='6eih' size='340' side='right' caption='[[6eih]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='6eih' size='340' side='right'caption='[[6eih]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6eih]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EIH FirstGlance]. <br>
<table><tr><td colspan='2'>[[6eih]] 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=6EIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EIH FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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]] 2.7&#8491;</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=6eih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eih OCA], [http://pdbe.org/6eih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eih RCSB], [http://www.ebi.ac.uk/pdbsum/6eih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eih ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=6eih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eih OCA], [https://pdbe.org/6eih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eih RCSB], [https://www.ebi.ac.uk/pdbsum/6eih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eih ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/1433E_HUMAN 1433E_HUMAN]] Distal 17p13.3 microdeletion syndrome;17p13.3 microduplication syndrome;Miller-Dieker syndrome.
[https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_HUMAN] Distal 17p13.3 microdeletion syndrome;17p13.3 microduplication syndrome;Miller-Dieker syndrome.  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/1433E_HUMAN 1433E_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.  
[https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ultraviolet (UV) light radiation induces the formation of bulky photoproducts in the DNA that globally affect transcription and splicing. However, the signaling pathways and mechanisms that link UV-light-induced DNA damage to changes in RNA metabolism remain poorly understood. Here we employ quantitative phosphoproteomics and protein kinase inhibition to provide a systems view on protein phosphorylation patterns induced by UV light and uncover the dependencies of phosphorylation events on the canonical DNA damage signaling by ATM/ATR and the p38 MAP kinase pathway. We identify RNA-binding proteins as primary substrates and 14-3-3 as direct readers of p38-MK2-dependent phosphorylation induced by UV light. Mechanistically, we show that MK2 phosphorylates the RNA-binding subunit of the NELF complex NELFE on Serine 115. NELFE phosphorylation promotes the recruitment of 14-3-3 and rapid dissociation of the NELF complex from chromatin, which is accompanied by RNA polymerase II elongation.
 
p38-MK2 signaling axis regulates RNA metabolism after UV-light-induced DNA damage.,Borisova ME, Voigt A, Tollenaere MAX, Sahu SK, Juretschke T, Kreim N, Mailand N, Choudhary C, Bekker-Jensen S, Akutsu M, Wagner SA, Beli P Nat Commun. 2018 Mar 9;9(1):1017. doi: 10.1038/s41467-018-03417-3. PMID:29523821<ref>PMID:29523821</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6eih" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Akutsu, M]]
[[Category: Homo sapiens]]
[[Category: Beli, P]]
[[Category: Large Structures]]
[[Category: Wagner, S A]]
[[Category: Akutsu M]]
[[Category: 14-3-3]]
[[Category: Beli P]]
[[Category: Nelf]]
[[Category: Wagner SA]]
[[Category: Protein binding]]
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