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| | <StructureSection load='4qun' size='340' side='right'caption='[[4qun]], [[Resolution|resolution]] 1.86Å' scene=''> | | <StructureSection load='4qun' size='340' side='right'caption='[[4qun]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qun]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QUN FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b49|2b49]], [[4qum|4qum]]</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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPH1, PTPN3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=4qun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qun OCA], [http://pdbe.org/4qun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qun RCSB], [http://www.ebi.ac.uk/pdbsum/4qun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qun ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTN3_HUMAN PTN3_HUMAN]] May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tyrosine phosphatase|Tyrosine phosphatase]] | + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]]
| + | [[Category: Chen KE]] |
| - | [[Category: Chen, K E]] | + | [[Category: Meng TC]] |
| - | [[Category: Meng, T C]] | + | [[Category: Wang AHJ]] |
| - | [[Category: Wang, A H.J]] | + | |
| - | [[Category: Alpha beta]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
PTN3_HUMAN May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen KE, Lin SY, Wu MJ, Ho MR, Santhanam A, Chou CC, Meng TC, Wang AH. Reciprocal allosteric regulation of p38gamma and PTPN3 involves a PDZ domain-modulated complex formation. Sci Signal. 2014 Oct 14;7(347):ra98. doi: 10.1126/scisignal.2005722. PMID:25314968 doi:http://dx.doi.org/10.1126/scisignal.2005722
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