Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and Its Substrate-trapping Mutants
نویسندگان
چکیده
منابع مشابه
Protein Tyrosine Phosphatase 1B Inhibitors: Catechols
As most intracellular signaling takes place via cascades of phosphorylation and dephosphorylation of tyrosines, protein tyrosine phosphatases have emerged as new and promising targets. Among them, protein tyrosine phosphatase 1B (PTP1B) negatively regulates insulin signaling by dephosphorylation of key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor, ther...
متن کاملPodocyte Protein, Nephrin, Is a Substrate of Protein Tyrosine Phosphatase 1B
Glomerular podocytes are critical for the barrier function of the glomerulus in the kidney and their dysfunction causes protein leakage into the urine (proteinuria). Nephrin is a key podocyte protein, which regulates the actin cytoskeleton via tyrosine phosphorylation of its cytoplasmic domain. Here we report that two protein tyrosine phosphatases, PTP1B and PTP-PEST negatively regulate nephrin...
متن کاملMolecular dynamics simulations of protein-tyrosine phosphatase 1B. II. substrate-enzyme interactions and dynamics.
Molecular dynamics simulations of protein tyrosine phosphatase 1B (PTP1B) complexed with the phosphorylated peptide substrate DADEpYL and the free substrate have been conducted to investigate 1) the physical forces involved in substrate-protein interactions, 2) the importance of enzyme and substrate flexibility for binding, 3) the electrostatic properties of the enzyme, and 4) the contribution ...
متن کاملAssessment of protein-tyrosine phosphatase 1B substrate specificity using "inverse alanine scanning".
An "inverse alanine scanning" peptide library approach has been developed to assess the substrate specificity of protein-tyrosine phosphatases (PTPases). In this method each Ala moiety in the parent peptide, Ac-AAAApYAAAA-NH(2), is separately and sequentially replaced by the 19 non-Ala amino acids to generate a library of 153 well defined peptides. The relatively small number of peptides allows...
متن کاملDominant role of the protein-tyrosine phosphatase CD148 in regulating platelet activation relative to protein-tyrosine phosphatase-1B.
OBJECTIVE The receptor-like protein-tyrosine phosphatase (PTP) CD148 and the nontransmembrane PTP1-B have been shown to be net positive regulators of Src family kinases in platelets. In the present study, we compared the relative contributions of these PTPs in platelet activation by the major glycoprotein, glycoprotein VI, α(IIb)β(3), and C-type lectin-like receptor 2 (CLEC-2). METHODS AND RE...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.m004490200