Fragment Screening and Assembly: A Highly Efficient Approach to a Selective and Cell Active Protein Tyrosine Phosphatase 1B Inhibitor
Journal of Medicinal Chemistry2003Vol. 46(20), pp. 4232–4235
Citations Over TimeTop 10% of 2003 papers
Gang Liu, Zhili Xin, Zhonghua Pei, Philip J. Hajduk, Cele Abad‐Zapatero, Charles W. Hutchins, Hongyu Zhao, Thomas Lübben, Stephen J. Ballaron, Deanna L. Haasch, Wiweka Kaszubska, Cristina M. Rondinone, James M. Trevillyan, Michael R. Jirousek
Abstract
Using an NMR-based fragment screening and X-ray crystal structure-based assembly, starting with millimolar ligands for both the catalytic site and the second phosphotyrosine binding site, we have identified a small-molecule inhibitor of protein tyrosine phosphatase 1B with low micromolar inhibition constant, high selectivity (30-fold) over the highly homologous T-cell protein tyrosine phosphatase, and good cellular activity in COS-7 cells.
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