| dc.description.abstract | Insulin receptor is a key component of insulin signaling pathway, playing a
crucial role in cellular metabolism, growth, and glucose homeostasis, and
regulated by dephosphorylation activity of protein tyrosine phosphatases,
especially protein tyrosine phosphatase 1B (PTP1B). Inhibition of molecular
interaction between PTP1B and insulin receptor kinase domain (IRK) has been
considered as a potential strategy to treat type 2 diabetes patients with insulin
resistance. Although the crystal structure of the PTP1B-IRK complex was solved,
the binding sites were not consistent with some prior experimental studies,
which provided evidences for PTP1B binding to the activation loop of IRK. This
has raised an interesting problem if the obtained structure is a stable
conformation in physiological condition or just a product of experimental
condition. Using three docking methods combined with interaction analysis, we
predicted the binding sites of PTP1B on the IRK activation loop, and reconfirmed
the importance of phosphotyrosine residues in the PTP1B-IRK complex.
KEYWORDS: Insulin Receptor Kinase, Protein Tyrosine Phospatase 1B, IRK,
PTP1B, Type 2 Diabetes, Molecular Docking | en_US |
