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

Structure

Volumn 5, Issue 5, 1997, Pages 601-612

  Urzhumtsev, A ^a,c   Tete Favier F ^a,d   Mitschler, A ^a   Barbanton, J ^b   Barth, P ^a   Urzhumtseva, L ^a,c   Biellmann, J F ^a   Podjarny, A D ^a   Moras, D ^a  

^a UNIVERSITÉ DE STRASBOURG   (France)

^b LIPHA Industries   (France)

^c RUSSIAN ACADEMY OF SCIENCES   (Russian Federation)

^d Nancy University CNRS   (France)

Author keywords

aldose reductase; crystal structure; diabetes; inhibitors

Indexed keywords

EID: 0031570301     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00216-5     Document Type: Article

References (40)

1. Larson, E.R., Lipinski, C.A. & Sarges, R. (1988). Medicinal chemistry of aldose reductase inhibitors. Med. Res. Rev. 8, 159-186.
2. Wermuth, B. & Monder, C. (1983). Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity. Eur. J. Biochem. 127, 279-284.
3. Warren, J.C., Murdock, G.M., Ma, Y., Goodman, S.R. & Zimmer, W.E. (1993). Molecular cloning of testicular 20-α hydroxysteroid dehydrogenase. Biochemistry 32, 1401-1406.
4. Branlant, G. (1982). Properties of an aldose reductase from pig lens. Eur. J. Biochem. 129, 99-104.
5. Hoffman, P.L., Wermuth, B. & Von Wartburg, J.-P. (1980). Human brain aldehyde reductases: relationship to succinil semi aldehyde reductase and aldose reductase. J. Neurochem. 35, 354-366.
6. Rondeau, J.-M., et al., & Moras, D. (1992). Novel NADPH binding domain revealed by the crystal structure of aldose reductase. Nature 355, 469-472.
7. Wilson, D.K., Bohren, K.M., Gabbay, K.H. & Quiocho F.A. (1992). An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257, 81-84.
8. Bohrani, D.W., Harter, T.M. & Petrash, J.M. (1992). The crystal structure of the aldose reductase -NADPH binary complex. J. Biol. Chem. 267, 24841-24847.
9. Tete, F., et al., & Moras, D. (1995). Aldose Reductase from Pig Lens. Eur. J. Med. Chem. 30 S, 589s-603s.
10. Varma, S.D., Mizuno, A. & Kinoshita, J.H. (1977). Diabetic cataracts and flavonoids. Science 195, 205-206.
11. Sarges, R., Bordner, J., Dominy, B.W., Peterson, M.J. & Whipple, E.B. (1985). Synthesis, absolute configuration, and conformation of the aldose reductase inhibitor sorbinil. J. Med. Chem. 28, 1716-1720.
12. York, B.M. (1983). Spirotricyclic aromatic succinimide derivates as inhibitors of aldose reductase, European Patent Application 0092385.
13. Dvornik, D., et al., & Merola, L. (1973). Polyol accumulation in galactodemic and diabetic rats: control by an aldose reductase inhibitor. Science 182, 1146-1147.
14. Sestanj, K., et al., & Dvornik, D. (1984). N-[5-(trifluoromethyl)-6-methoxy-1-naphthalenyl] thioxomethyl]- N- methylglycine (Tolrestat), a potent, orally active aldose reductase inhibitor. J. Med. Chem. 27, 255-256.
15. Macleod, A.F., et al., & Van Der Veen, E.A. (1992). A multicentre trial of the aldose-reductase inhibitor tolrestat, in patients with symptomatic diabetic peripheral neuropathy. North European Tolrestat Study Group Diabetes Metab. 18, 14-20.
16. Stribling, D., Mirrlees, D.J., Harrison, H.E. & Earl, D.C.N. (1985). Properties of ICI 128,436, a novel aldose reductase inhibitor, and its effects on diabetic complications in the rat. Metabolism 34, 336-344.
17. Sarges, R. & Dates, P.J. (1993). Aldose reductase inhibitors: recent developments. Prog. Drug. Res. 40, 99-161.
18. Hotta, N., Kakuta, H., Ando, F. & Sakamoto, N. (1990). Current progress in clinical trials of aldose reductase inhibitors in Japan. Exp. Eye Res. 50, 625-628.
19. Ward, W.H., et al., & Howe, R. (1991). (2,6 dimethylphenylsulfonyl) nitromethane: a new structural type of aldose reductase inhibitor which follows biphasic kinetics and uses an allosteric binding site. Biochem. Pharmacol. 42, 2115-2123.
20. Cook, P.N., et al., & Howe, R. (1995). Kinetic characteristics of Zeneca ZD5522, a potent inhibitor of human and bovine lens aldose reductase. Biochem. Pharmacol. 49, 1043-1049.
21. Wilson, D.K., Tarle, I., Petrash, J.M. & Quiocho, F.A. (1993). Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. USA 90, 9847-9851.
22. Harrison, D.H., Bohern, K.M., Ringe, D., Petsko, G.A. & Gabbay, K.H. (1994). An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry 33, 2011-2020.
23. Nakano, T. & Petrash, J.M. (1996). Kinetic and spectroscopic evidence for active site inhibition of human aldose reductase. Biochemistry 35, 11196-11202.
24. Kubiseski, T.J., Hyndman, D.J., Morjana, N.A. & Flynn, T.G. (1992). Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for slow conformational change upon coenzyme binding. J. Biol. Chem. 267, 6510-6517.
25. Grimshaw, C.E., Shahbaz, M. & Putney, C.G. (1990). Mechanistic basis for non-linear kinetics of aldehyde reduction catalysed by aldose reductase. Biochemistry 29, 9947-9955.
26. De Winter, H.L. &von Itzstein, M. (1995). Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme. Biochemistry 34, 8299-8308.
27. Rarey, M., Kramer, B., Lengauer, T. & Klebe, G. (1996). A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261, 470-489.
28. +/NADPH and alrestatin-like inhibitors. Biochemistry 33, 7157-7165.
29. Barski, O.A., Gabbay, K.H., Grimshaw, C.E. & Bohren K.M. (1995). Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34, 11264-11275.
30. Reymann, J.M., Rondeau, J.-M., Barth, P., Jacquinod, M., van Dorsselaer, A. & Biellmann, J.-F. (1992). Purification and electrospray mass spectrometry of aldose reductase from pig lens. Biochem. Biophys. Acta 1122, 1-5.
31. Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a position sensitive detector. J. Appl. Cryst. 21, 916-924.
32. Brünger, A.T. (1992). X-PLOR, Version 3.1: A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT, USA.
33. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M.O. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
34. Urzhumtsev, A.G., Skovoroda, T.P. & Lunin, V.Yu. (1996). A procedure compatible with X-PLOR for the calculation of electron-density maps weighted using an R-free-likelihood based approach. J. Appl. Cryst. 29, 741-744.
35. Kleywegt, G.J. & Jones, T.A. (1996). xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflections data sets. Acta Cryst. D 52, 826-828.
36. Program Manual for the Wisconsin Package, Version 8, August 1994. 575 Science Drive, Madison, Wisconsin, USA 53711.
37. Evans, S.V. (1993). SETOR: hardware lighted three dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
38. Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
39. +, NADH, and the pyrophosphate groups of nucleotides. J. Comput. Chem. 18, 221-239.
40. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1991). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.