8c2d

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Current revision (12:35, 26 July 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8c2d is ON HOLD until Paper Publication
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==14-3-3 in complex with Pyrin pS208==
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<StructureSection load='8c2d' size='340' side='right'caption='[[8c2d]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8c2d]] 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=8C2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C2D 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]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=8c2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c2d OCA], [https://pdbe.org/8c2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c2d RCSB], [https://www.ebi.ac.uk/pdbsum/8c2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c2d 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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Overactivation of Pyrin is the cause of the inflammatory diseases Mediterranean Fever and Pyrin-associated autoinflammation with neutrophilic dermatosis (PAAND). Binding of 14-3-3 proteins reduces the pro-inflammatory activity of Pyrin, hence small molecules that stabilize the Pyrin/14-3-3 complex could convey an anti-inflammatory effect. We have solved the atomic resolution crystal structures of phosphorylated peptides derived from PyrinpS208 and PyrinpS242 - the two principle 14-3-3 binding sites in Pyrin - in complex with 14-3-3 and analyzed the ligandability of these protein-peptide interfaces by crystal-based fragment soaking. The complex between 14-3-3 and PyrinpS242 appears to be much more amenable for small-molecule binding than that of 14-3-3/PyrinpS208. Consequently, only for the 14-3-3/PyrinpS242 complex could we find an interface-binding fragment, validating protein crystallography and fragment soaking as a method to evaluate the ligandability of protein surfaces.
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Authors: Lau, R., Ottmann, C., Hann, M.
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Crystal structure and ligandability of the 14-3-3/pyrin interface.,Lau R, Hann MM, Ottmann C Biochem Biophys Res Commun. 2023 Apr 9;651:1-7. doi: 10.1016/j.bbrc.2023.02.013. , Epub 2023 Feb 4. PMID:36774661<ref>PMID:36774661</ref>
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Description: 14-3-3 in complex with Pyrin pS208
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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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[[Category: Ottmann, C]]
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<div class="pdbe-citations 8c2d" style="background-color:#fffaf0;"></div>
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[[Category: Lau, R]]
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== References ==
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[[Category: Hann, M]]
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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: Hann M]]
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[[Category: Lau R]]
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[[Category: Ottmann C]]

Current revision

14-3-3 in complex with Pyrin pS208

PDB ID 8c2d

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