5glj: Difference between revisions

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== Function ==
== Function ==
[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>  
[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>  
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== 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<ref>PMID:27544031</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==

Latest revision as of 12:12, 20 March 2024

Crystal Structure of PDZ1 Domain of Human Protein Tyrosine Phosphatase PTP-BasCrystal Structure of PDZ1 Domain of Human Protein Tyrosine Phosphatase PTP-Bas

Structural highlights

5glj is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTN13_HUMAN Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.[1]

See Also

References

  1. 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

5glj, resolution 1.60Å

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OCA