5j8r

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(New page: ==Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant== <StructureSection load='5j8r' size='340' side='right' caption='[[5j8...)
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==Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant==
==Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant==
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<StructureSection load='5j8r' size='340' side='right' caption='[[5j8r]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
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<StructureSection load='5j8r' size='340' side='right'caption='[[5j8r]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5j8r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J8R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5j8r]] is a 4 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=5J8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J8R FirstGlance]. <br>
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</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>
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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]] 2.043&#8491;</td></tr>
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<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=5j8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8r OCA], [http://pdbe.org/5j8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8r RCSB], [http://www.ebi.ac.uk/pdbsum/5j8r PDBsum]</span></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=5j8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8r OCA], [https://pdbe.org/5j8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j8r RCSB], [https://www.ebi.ac.uk/pdbsum/5j8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PTN12_HUMAN PTN12_HUMAN]] Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.<ref>PMID:17329398</ref>
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[https://www.uniprot.org/uniprot/PTN12_HUMAN PTN12_HUMAN] Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.<ref>PMID:17329398</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PTPN12 is an important tumor suppressor that plays critical roles in various physiological processes. However, the molecular basis underlying the substrate specificity of PTPN12 remains uncertain. Here, enzymological and crystallographic studies have enabled us to identify two distinct structural features that are crucial determinants of PTPN12 substrate specificity: the pY+1 site binding pocket and specific basic charged residues along its surface loops. Key structurally plastic regions and specific residues in PTPN12 enabled recognition of different HER2 phosphorylation sites and regulated specific PTPN12 functions. In addition, the structure of PTPN12 revealed a CDK2 phosphorylation site in a specific PTPN12 loop. Taken together, our results not only provide the working mechanisms of PTPN12 for desphosphorylation of its substrates but will also help in designing specific inhibitors of PTPN12.
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Crystal Structure and Substrate Specificity of PTPN12.,Li H, Yang F, Liu C, Xiao P, Xu Y, Liang Z, Liu C, Wang H, Wang W, Zheng W, Zhang W, Ma X, He D, Song X, Cui F, Xu Z, Yi F, Sun JP, Yu X Cell Rep. 2016 May 10;15(6):1345-58. doi: 10.1016/j.celrep.2016.04.016. Epub 2016, Apr 28. PMID:27134172<ref>PMID:27134172</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5j8r" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Homo sapiens]]
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[[Category: Li, H]]
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[[Category: Large Structures]]
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[[Category: Sun, J P]]
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[[Category: Li H]]
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[[Category: Wang, W J]]
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[[Category: Sun JP]]
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[[Category: Xiao, P]]
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[[Category: Wang WJ]]
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[[Category: Xu, Y F]]
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[[Category: Xiao P]]
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[[Category: Yang, F]]
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[[Category: Xu YF]]
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[[Category: Yu, X]]
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[[Category: Yang F]]
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[[Category: Cancer]]
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[[Category: Yu X]]
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[[Category: Hydrolase]]
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[[Category: Tyrosine phosphorylation]]
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Current revision

Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant

PDB ID 5j8r

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