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• W2067156966 startingPage "1643" @default.
• W2067156966 abstract "Protein tyrosine phosphatase 1B (PTP1B) is a highly specific negative regulator of insulin receptor signaling in vivo. The determinants of PTP1B specificity for the insulin receptor versus other receptor tyrosine kinases are largely unknown. Here, we report a crystal structure at 2.3 Å resolution of the catalytic domain of PTP1B (trapping mutant) in complex with the phosphorylated tyrosine kinase domain of the insulin receptor (IRK). The crystallographic asymmetric unit contains two PTP1B-IRK complexes that interact through an IRK dimer interface. Rather than binding to a phosphotyrosine in the IRK activation loop, PTP1B binds instead to the opposite side of the kinase domain, with the phosphorylated activation loops sequestered within the IRK dimer. The crystal structure provides evidence for a noncatalytic mode of interaction between PTP1B and IRK, which could be important for the selective recruitment of PTP1B to the insulin receptor." @default.
• W2067156966 created "2016-06-24" @default.
• W2067156966 creator A5004591046 @default.
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• W2067156966 date "2005-11-01" @default.
• W2067156966 modified "2023-10-11" @default.
• W2067156966 title "Crystal Structure of a Complex between Protein Tyrosine Phosphatase 1B and the Insulin Receptor Tyrosine Kinase" @default.
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• W2067156966 doi "https://doi.org/10.1016/j.str.2005.07.019" @default.
• W2067156966 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16271887" @default.
• W2067156966 hasPublicationYear "2005" @default.
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