Studies on the inhibitor-binding site of porcine aldehyde reductase: Crystal structure of the holoenzyme-inhibitor ternary complex

Proteins: Structure, Function and Genetics

Volumn 29, Issue 2, 1997, Pages 186-192

  El Kabbani, Ossama ^a   Carper, Deborah A ^b   McGowan, Michelle H ^b   Devedjiev, Yancho ^c   Rees Milton, Karen J ^d   Flynn, T Geoffrey ^d  

^a MONASH UNIVERSITY   (Australia)

^b NATIONAL EYE INSTITUTE   (United States)

^c UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^d QUEEN S UNIVERSITY   (Canada)

Author keywords

barrel; Aldo keto reductase; Diabetic complications; Drug design; Site directed mutagenesis; X ray crystallography

Indexed keywords

ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; RECOMBINANT PROTEIN; TOLRESTAT;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DIABETES MELLITUS; ENZYME ACTIVE SITE; ENZYME INHIBITOR COMPLEX; ENZYME PURIFICATION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SWINE; X RAY CRYSTALLOGRAPHY;

ALDEHYDE REDUCTASE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; MOLECULAR STRUCTURE; NAPHTHALENES; SWINE;

SUIDAE; SUS SCROFA;

EID: 0030982582     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199710)29:2<186::AID-PROT6>3.0.CO;2-B     Document Type: Article

References (33)

1. Flynn, T.G. Aldehyde reductases: monomeric NADPH-dependent oxidoreductases with multifunctional potential. Biochem. Pharmacol. 31:2705-2712, 1982.
2. Wermuth, B. In: "Enzymology and Molecular Biology of Carbonyl Metabolism." Flynn, T.G., Weiner, H. (eds.). New York: Alan Liss, 1985:209-230.
3. Bohren, K.M., Bullock, B., Wermuth, B., Gabbay, K.H. The aldo-keto reductases superfamily. J. Biol. Chem. 264:9547-9551, 1989.
4. Kinoshita, J.H., Nishimura, C. The involvement of aldose reductase in diabetic complications. Diabetes Metab. Rev. 4:323-337, 1988.
5. Srivastava, S.K., Petrash, J.M., Sadana, I.J., Ansari, N.H., Partridge, C.A. Susceptibility of aldehyde and aldose reductases of human tissues to aldose reductase inhibitors. Curr. Eye Res. 83:407-410, 1982.
6. Speilberg, S.P., Shear, N.H., Cannon, M., Huston, N.J., Gunderson, K. In-vitro assessment of a hypersensitivity syndrome associated with sorbinil. Ann. Intern. Med. 114:720-724, 1991.
7. Sarges, R., Oates, P. Aldose reductase inhibitors: Recent developments. J. Prog. Drug Res. 40:99-161, 1993.
8. Sato, S., Kador, P. Inhibition of aldehyde reductase by aldose reductase inhibitors. Biochem. Pharmacol. 40:1033-1042, 1990.
9. Wilson, D.K., Tarle, I., Petrash, J.M., Quiocho, F.A. Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. 90:9847-9851, 1993.
10. +/NADPH and alrestatin-like inhibitors. Biochemistry 33:7157-7165, 1994.
11. Barski, O., Gabbay, K.H., Grimshaw, C.E., Bohren, K.M. Mechanism of human aldehyde reductase: Characterization of the active site pocket. Biochemistry 34:11264-11275, 1995.
12. El-Kabbani, O., Green, N.C., Lin, G., Carson, M., Narayana, S.V.L., Moore, K.M., Flynn, T.G., DeLucas, L.J. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr. D50:859-868, 1994.
13. El-Kabbani, O., Judge, K., Ginell, S.L., Myles, D.A.A., DeLucas, L.J., Flynn, T.G. Structure of porcine aldehyde reductase holoenzyme. Nature Struct. Biol. 2:687-692, 1995.
14. Rondeau, J.-M., Tête-Favier, F., Podjarny, A., Reymann, J.-M., Barth, P., Biellmann, J.F., Moras, D. Novel NADPH binding domain revealed by the crystal structure of aldose reductase. Nature (Lond.) 355:469-472, 1992.
15. Wilson, D.K., Bohren, K.M., Gabbay, K.H., Quiocho, F.A. An unlikely sugar substrate site in the 1.65 Å structure of human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84, 1992.
16. Wermuth, B. In: "Enzymology and Molecular Biology of Carbonyl Metabolism." Weiner, H., Wermuth, B. (eds). New York: Alan Liss, 1992:261-274.
17. Green, N.C. "Studies on the Structure, Expression and Mechanism of Aldo-Keto Reductases." Ph.D. Thesis, Department of Biochemistry, Queen's University, Kingston, Ontario, Canada, 1995.
18. Carper, D.A., Hohman, T.C., Old, S.E. Residues affecting the catalysis and inhibition of rat lens aldose reductase. Biochim. Biophys. Acta 1246:67-73, 1995.
19. Bohren, K.M., Grimshaw, C.E., Lai, C.-J., Harrison, D.H., Ringe, D., Petsko, G.A., Gabbay, K.H. Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: Enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33:2021-2032, 1994.
20. Tarle, I., Borhani, D.W., Wilson, D.K., Quiocho, F.A., Petrash, J.M. Probing the active site of human aldose reductase: Site directed mutagenesis of Asp-43, Tyr-48, Lys-77 and His-110. J. Biol. Chem. 268:25687-25693, 1993.
21. El-Kabbani, O., Carper, D.A., McGowan, M.H., Ginell, S.L. Crystal structure of porcine aldehyde reductase at 2.0 Å resolution: modeling an inhibitor in the active site of the enzyme. Protein Pept. Lett. 3:427-434, 1996.
22. Cromlish, J.A., Flynn, T.G. Pig muscle aldehyde reductase. Identity of pig muscle aldehyde reductase with pig lens aldose reductase and with low Km aldehyde reductase of pig brain and pig kidney. J. Biol. Chem. 258:3583-3586, 1983.
23. McPherson, A. Crystallization of macromolecules: general principles. Methods Enzymol. 114:112-120, 1985.
24. Howard, A.J., Gilliand, G.L., Finzel, B.C., Poulos, T.L., Ohlendorf, D.H., Salemme, F.R. The use of an imaging proportional counter in macromolecular crystallography. J. Appl. Crystallogr. 20:383-387, 1987.
25. Cambillau, C.M. Tom, molecular graphics program for Silicon Graphics Iris series, version 2.4, 1987.
26. Brünger, A.T., Krukowski, A., Erickson, J. Slow-cooling protocol for crystallographic refinement by simulated annealing. Acta Crystallogr. A46:585-593, 1990.
27. Luzzati, V. Traitement statistique des erreurs dans las détérmination des structures cristalline. Acta Crystallogr. 5:802-810, 1952.
28. Jones, D.H., Howard, B.H. A rapid method for site-specific mutagenesis and directional subcloning by using the polymerase chain reaction to generate recombinant circles. Bio/Techniques 8:178-183, 1990.
29. i. Biochem. J. 129:197-202, 1972.
30. Barski, O.A., Gabbay, K.H., Bohren, K.M. The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry 35:14276-14280, 1996.
31. De Winter, H.L., von Itzstein, M. 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, 1995.
32. 2. Can. J. Chem. 61:2137-2140, 1983.
33. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950, 1991.