Target-specific control of lymphoid-specific protein tyrosine phosphatase (Lyp) activity
نویسندگان
چکیده
منابع مشابه
Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp.
Protein tyrosine phosphatases act in conjunction with protein kinases to regulate the tyrosine phosphorylation events that control cell activation and differentiation. We have isolated a previously undescribed human phosphatase, Lyp, that encodes an intracellular 105-kD protein containing a single tyrosine phosphatase catalytic domain. The noncatalytic domain contains four proline-rich potentia...
متن کاملStructure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases.
The lymphoid-specific tyrosine phosphatase (Lyp) has generated enormous interest because a single-nucleotide polymorphism in the gene (PTPN22) encoding Lyp produces a gain-of-function mutant phosphatase that is associated with several autoimmune diseases, including type I diabetes, rheumatoid arthritis, Graves disease, and systemic lupus erythematosus. Thus, Lyp represents a potential target fo...
متن کاملBiochemical and Functional Studies of Lymphoid-Specific Tyrosine Phosphatase (Lyp) Variants S201F and R266W
The Lymphoid specific tyrosine phosphatase (Lyp) has elicited tremendous research interest due to the high risk of its missense mutation R620W in a wide spectrum of autoimmune diseases. While initially characterized as a gain-of-function mutant, R620W was thought to lead to autoimmune diseases through loss-of-function in T cell signaling by a recent study. Here we investigate the biochemical ch...
متن کاملPeptide-based activity-based probes (ABPs) for target-specific profiling of protein tyrosine phosphatases (PTPs).
Synthesis of a novel unnatural amino acid (2-FMPT) for the solid-phase synthesis of peptide-based probes suitable for target-specific activity-based profiling of protein tyrosine phosphatases from crude proteomes is reported.
متن کاملChemical rescue of protein tyrosine phosphatase activity.
We report that the activity of a rationally engineered protein tyrosine phosphatase (PTP) mutant can be fully rescued by the addition of the biarsenical fluorescein derivative FlAsH, a compound that does not affect the activity of wild-type PTPs.
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ژورنال
عنوان ژورنال: Bioorganic & Medicinal Chemistry
سال: 2010
ISSN: 0968-0896
DOI: 10.1016/j.bmc.2010.06.022