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Discovery of covalent inhibitors for MIF tautomerase via cocrystal structures with phantom hits from virtual screening.

McLean LR, Zhang Y, Li H, Li Z, Lukasczyk U, Choi YM, Han Z, Prisco J, Fordham J, Tsay JT, Reiling S, Vaz RJ, Li Y
Bioorg Med Chem Lett 19 6717-20 (2009)
Related entries: 3jsf, 3jtu

Cited: 20 times
EuropePMC logo PMID: 19836948

Abstract

Biochemical and X-ray crystallographic studies confirmed that hydroxyquinoline derivatives identified by virtual screening were actually covalent inhibitors of the MIF tautomerase. Adducts were formed by N-alkylation of the Pro-1 at the catalytic site with a loss of an amino group of the inhibitor.

Articles - 3jsg mentioned but not cited (2)

  1. Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel. Pantouris G, Khurana L, Ma A, Skeens E, Reiss K, Batista VS, Lisi GP, Lolis EJ. Cell Chem Biol 27 740-750.e5 (2020)
  2. Discovery of novel MIF inhibitors that attenuate microglial inflammatory activation by structures-based virtual screening and in vitro bioassays. Zhang Y, Xu L, Zhang Y, Pan J, Wang PQ, Tian S, Li HT, Gao BW, Hou TJ, Zhen XC, Zheng LT. Acta Pharmacol Sin 43 1508-1520 (2022)


Reviews citing this publication (1)

  1. Biophysical Survey of Small-Molecule β-Catenin Inhibitors: A Cautionary Tale. McCoy MA, Spicer D, Wells N, Hoogewijs K, Fiedler M, Baud MGJ. J Med Chem 65 7246-7261 (2022)

Articles citing this publication (17)



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