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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dhn]] is a 1 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=4DHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DHN FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dhn]] is a 1 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=4DHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DHN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0KC:{2-[2-(CYCLOPENTYLAMINO)-2-OXOETHOXY]PHENYL}PHOSPHONIC+ACID'>0KC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0KC:{2-[2-(CYCLOPENTYLAMINO)-2-OXOETHOXY]PHENYL}PHOSPHONIC+ACID'>0KC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4dhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dhn OCA], [https://pdbe.org/4dhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dhn RCSB], [https://www.ebi.ac.uk/pdbsum/4dhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dhn 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=4dhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dhn OCA], [https://pdbe.org/4dhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dhn RCSB], [https://www.ebi.ac.uk/pdbsum/4dhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dhn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity).  p53-regulated inhibitor of G2/M progression.
[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity).  p53-regulated inhibitor of G2/M progression.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report first non-covalent and exclusively extracellular inhibitors of 14-3-3 protein-protein interactions identified by virtual screening. Optimization by crystal structure analysis and in vitro binding assays yielded compounds capable of disrupting the interaction of 14-3-3sigma with aminopeptidase N in a cellular assay.
 
Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 protein-protein interactions.,Thiel P, Roglin L, Meissner N, Hennig S, Kohlbacher O, Ottmann C Chem Commun (Camb). 2013 Aug 27;49(76):8468-70. doi: 10.1039/c3cc44612c. PMID:23939230<ref>PMID:23939230</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dhn" style="background-color:#fffaf0;"></div>


==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 ==
<references/>
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</StructureSection>
</StructureSection>
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