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8r0z

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Current revision (05:34, 4 September 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8r0z is ON HOLD until Paper Publication
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==14-3-3 sigma in complex with TAZ peptide and stabilizing fragment TCF199==
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<StructureSection load='8r0z' size='340' side='right'caption='[[8r0z]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8r0z]] 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=8R0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8R0Z FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</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=8r0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8r0z OCA], [https://pdbe.org/8r0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8r0z RCSB], [https://www.ebi.ac.uk/pdbsum/8r0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8r0z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The identification of chemical starting points for the development of molecular glues is challenging. Here, we employed fragment screening and identified an allosteric stabilizer of the complex between 14-3-3 and a TAZ-derived peptide. The fragment binds preferentially to the 14-3-3/TAZ peptide complex and shows moderate stabilization in differential scanning fluorimetry and microscale thermophoresis. The binding site of the fragment was predicted by molecular dynamics calculations to be distant from the 14-3-3/TAZ peptide interface, located between helices 8 and 9 of the 14-3-3 protein. This site was confirmed by nuclear magnetic resonance and X-ray protein crystallography, revealing the first example of an allosteric stabilizer for 14-3-3 protein-protein interactions.
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Authors:
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Fragment-Based Interrogation of the 14-3-3/TAZ Protein-Protein Interaction.,Andlovic B, Valenti D, Centorrino F, Picarazzi F, Hristeva S, Hiltmann M, Wolf A, Cantrelle FX, Mori M, Landrieu I, Levy LM, Klebl B, Tzalis D, Genski T, Eickhoff J, Ottmann C Biochemistry. 2024 Sep 3;63(17):2196-2206. doi: 10.1021/acs.biochem.4c00248. Epub , 2024 Aug 22. PMID:39172504<ref>PMID:39172504</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8r0z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Andlovic B]]
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[[Category: Centorrino F]]
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[[Category: Ottmann C]]

Current revision

14-3-3 sigma in complex with TAZ peptide and stabilizing fragment TCF199

PDB ID 8r0z

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