4rh5: Difference between revisions
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<StructureSection load='4rh5' size='340' side='right'caption='[[4rh5]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4rh5' size='340' side='right'caption='[[4rh5]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rh5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RH5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rh5]] 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=4RH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RH5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh5 OCA], [https://pdbe.org/4rh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rh5 RCSB], [https://www.ebi.ac.uk/pdbsum/4rh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rh5 ProSAT]</span></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=4rh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh5 OCA], [https://pdbe.org/4rh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rh5 RCSB], [https://www.ebi.ac.uk/pdbsum/4rh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rh5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 29: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen K-E]] | |||
[[Category: Chen | [[Category: Meng TC]] | ||
[[Category: Meng | [[Category: Wang AH-J]] | ||
[[Category: Wang | |||
Latest revision as of 18:15, 8 November 2023
Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 peptideCrystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 peptide
Structural highlights
FunctionPTN3_HUMAN May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. Publication Abstract from PubMedEpidermal growth factor receptor (EGFR) pathway substrate 15 (Eps15) is a newly identified substrate for protein tyrosine phosphatase N3 (PTPN3), which belongs to the FERM-containing PTP subfamily comprising five members including PTPN3, N4, N13, N14, and N21. We solved the crystal structures of the PTPN3-Eps15 phosphopeptide complex and found that His812 of PTPN3 and Pro850 of Eps15 are responsible for the specific interaction between them. We defined the critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. We identified that Glu instead of Asp in the WPE loop contributes to the catalytic incapability of PTPN21 due to an extended distance beyond protonation targeting a phosphotyrosine substrate. Together with in vivo validations, our results provide novel insights into the substrate specificity and plasticity of FERM-containing PTPs. Substrate Specificity and Plasticity of FERM-Containing Protein Tyrosine Phosphatases.,Chen KE, Li MY, Chou CC, Ho MR, Chen GC, Meng TC, Wang AH Structure. 2015 Feb 18. pii: S0969-2126(15)00041-6. doi:, 10.1016/j.str.2015.01.017. PMID:25728925[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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