A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.

@article{Urzhumtsev1997AP,
  title={A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.},
  author={Alexandre Urzhumtsev and Fr{\'e}d{\'e}rique T{\^e}te-Favier and Andr{\'e} Mitschler and Jacques Barbanton and Patrick Barth and Ludmila Urzhumtseva and Jean François Biellmann and Alberto D. Podjarny and Dino Moras},
  journal={Structure},
  year={1997},
  volume={5 5},
  pages={
          601-12
        }
}
  • Alexandre Urzhumtsev, Frédérique Tête-Favier, +6 authors Dino Moras
  • Published in Structure 1997
  • Chemistry, Medicine
  • BACKGROUND Aldose reductase (AR) is an NADPH-dependent enzyme implicated in long-term diabetic complications. Buried at the bottom of a deep hydrophobic cleft, the NADPH coenzyme is surrounded by the conserved hydrophilic residues of the AR active site. The existence of an anionic binding site near the NADP+ has been determined from the structures of the complexes of AR with citrate, cacodylate and glucose-6-phosphate. The inhibitor zopolrestat binds to this anionic site, and in the hydrophobic… CONTINUE READING

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