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| | <StructureSection load='5glj' size='340' side='right'caption='[[5glj]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5glj' size='340' side='right'caption='[[5glj]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5glj]] is a 4 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=5GLJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GLJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5glj]] 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=5GLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GLJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPN13, PNP1, PTP1E, PTPL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5glj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glj OCA], [https://pdbe.org/5glj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5glj RCSB], [https://www.ebi.ac.uk/pdbsum/5glj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5glj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5glj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glj OCA], [http://pdbe.org/5glj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5glj RCSB], [http://www.ebi.ac.uk/pdbsum/5glj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5glj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTN13_HUMAN PTN13_HUMAN]] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.<ref>PMID:15611135</ref> | + | [https://www.uniprot.org/uniprot/PTN13_HUMAN PTN13_HUMAN] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.<ref>PMID:15611135</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]]
| + | [[Category: Chi SW]] |
| - | [[Category: Chi, S W]] | + | [[Category: Ku B]] |
| - | [[Category: Ku, B]] | + | [[Category: Lee SO]] |
| - | [[Category: Lee, S O]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pdz1 domain]]
| + | |
| - | [[Category: Ptp-ba]]
| + | |
| Structural highlights
Function
PTN13_HUMAN Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.[1]
Publication Abstract from PubMed
Protein tyrosine phosphatase-Basophil (PTP-Bas) is a membrane-associated protein tyrosine phosphatase with five PDZ domains and is involved in apoptosis, tumorigenesis, and insulin signaling. The interaction between PTP-Bas and tandem-PH-domain-containing protein 1/2 (TAPP1/2) plays an essential role in the regulation of insulin signaling. Despite its high sequence homology with the other PDZ domains, only the PDZ1 domain of PTP-Bas showed distinct binding specificity for TAPP1/2. Although the interaction between PTP-Bas PDZ1 and TAPP1/2 is a therapeutic target for diabetes, the structural basis for the interaction has not been elucidated. In the present study, we determined the crystal structure of the PTP-Bas PDZ1 domain at 1.6 A resolution. In addition, we calculated the structural models of complexes of PTP-Bas PDZ1 and the C-terminal peptides of TAPP1/2 (referred to as TAPP1p/2p). Structural comparison with the PTP-Bas PDZ2/RA-GEF2 peptide complex revealed a structural basis for distinct binding specificity of PTP-Bas PDZ1 for TAPP1p/2p peptides. Our high-resolution crystal structure of PTP-Bas PDZ1 will serve as a useful template for rational structure-based design of novel anti-diabetes therapeutics.
High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas.,Lee SO, Lee MK, Ku B, Bae KH, Lee SC, Lim HM, Kim SJ, Chi SW Biochem Biophys Res Commun. 2016 Sep 23;478(3):1205-10. doi:, 10.1016/j.bbrc.2016.08.095. Epub 2016 Aug 18. PMID:27544031[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Villa F, Deak M, Bloomberg GB, Alessi DR, van Aalten DM. Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket. J Biol Chem. 2005 Mar 4;280(9):8180-7. Epub 2004 Dec 20. PMID:15611135 doi:10.1074/jbc.M412211200
- ↑ Lee SO, Lee MK, Ku B, Bae KH, Lee SC, Lim HM, Kim SJ, Chi SW. High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas. Biochem Biophys Res Commun. 2016 Sep 23;478(3):1205-10. doi:, 10.1016/j.bbrc.2016.08.095. Epub 2016 Aug 18. PMID:27544031 doi:http://dx.doi.org/10.1016/j.bbrc.2016.08.095
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