4qun
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the PTPN3 (PTPH1) catalytic domain C842S mutant== | |
| + | <StructureSection load='4qun' size='340' side='right'caption='[[4qun]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qun]] 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=4QUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QUN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4qun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qun OCA], [https://pdbe.org/4qun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qun RCSB], [https://www.ebi.ac.uk/pdbsum/4qun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qun ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PTN3_HUMAN PTN3_HUMAN] May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitogen-activated protein kinase p38gamma (also known as MAPK12) and its specific phosphatase PTPN3 (also known as PTPH1) cooperate to promote Ras-induced oncogenesis. We determined the architecture of the PTPN3-p38gamma complex by a hybrid method combining x-ray crystallography, small-angle x-ray scattering, and chemical cross-linking coupled to mass spectrometry. A unique feature of the glutamic acid-containing loop (E-loop) of the phosphatase domain defined the substrate specificity of PTPN3 toward fully activated p38gamma. The solution structure revealed the formation of an active-state complex between p38gamma and the phosphatase domain of PTPN3. The PDZ domain of PTPN3 stabilized the active-state complex through an interaction with the PDZ-binding motif of p38gamma. This interaction alleviated autoinhibition of PTPN3, enabling efficient tyrosine dephosphorylation of p38gamma. Our findings may enable structure-based drug design targeting the PTPN3-p38gamma interaction as an anticancer therapeutic. | ||
| - | + | Reciprocal allosteric regulation of p38gamma and PTPN3 involves a PDZ domain-modulated complex formation.,Chen KE, Lin SY, Wu MJ, Ho MR, Santhanam A, Chou CC, Meng TC, Wang AH Sci Signal. 2014 Oct 14;7(347):ra98. doi: 10.1126/scisignal.2005722. PMID:25314968<ref>PMID:25314968</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4qun" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen KE]] | ||
| + | [[Category: Meng TC]] | ||
| + | [[Category: Wang AHJ]] | ||
Current revision
Crystal structure of the PTPN3 (PTPH1) catalytic domain C842S mutant
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