High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas

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Title
High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas
Author(s)
Sang-Ok Lee; Mi-Kyung LeeBonsu KuKwang-Hee BaeSang Chul Lee; H M Lim; Seung Jun KimSeung-Wook Chi
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 478, pp. 1205-1210
Publication Year
2016
Abstract
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.
Keyword
Binding specificityCrystal structurePDZ domainProtein tyrosine phosphatase-BasophilTandem-PH-domain-containing protein-1
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2016.08.095
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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