[HTML][HTML] Structure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B
LF Iversen, HS Andersen, S Branner… - Journal of Biological …, 2000 - ASBMB
Several protein-tyrosine phosphatases (PTPs) have been proposed to act as negative
regulators of insulin signaling. Recent studies have shown increased insulin sensitivity and
resistance to obesity in PTP1B knockout mice, thus pointing to this enzyme as a potential
drug target in diabetes. Structure-based design, guided by PTP mutants and x-ray protein
crystallography, was used to optimize a relatively weak, nonphosphorus, nonpeptide
general PTP inhibitor (2-(oxalyl-amino)-benzoic acid) into a highly selective PTP1B inhibitor …
regulators of insulin signaling. Recent studies have shown increased insulin sensitivity and
resistance to obesity in PTP1B knockout mice, thus pointing to this enzyme as a potential
drug target in diabetes. Structure-based design, guided by PTP mutants and x-ray protein
crystallography, was used to optimize a relatively weak, nonphosphorus, nonpeptide
general PTP inhibitor (2-(oxalyl-amino)-benzoic acid) into a highly selective PTP1B inhibitor …