Ligand-based protein alignment and isozyme specificity of glutathione S- transferase inhibitors

Proteins: Structure, Function and Genetics

Volumn 28, Issue 2, 1997, Pages 202-216

  Koehler, Ryan T ^a   Villar, Hugo O ^a   Bauer, Karin E ^a   Higgins, Deborah L ^a  

^a Terrapin Technologies Inc   (United States)

Author keywords

Analogues; Bound ligands; Isozymes; Model compounds

Indexed keywords

ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; LIGAND;

ARTICLE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; ENZYME SPECIFICITY; LIGAND BINDING; LIPOPHILICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING, COMPETITIVE; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GLUTATHIONE TRANSFERASE; HUMANS; HYDROGEN BONDING; ISOENZYMES; LIGANDS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

EID: 0031010027     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<202::AID-PROT9>3.0.CO;2-G     Document Type: Article

References (46)

1. Mannervik, B., Danielson, U.K. Glutathione transferases: Structure and catalytic activity. CRC Crit. Rev. Biochem. 23:283-337, 1988.
2. Jacoby, W.B., Ziegler, D.M. The enzymes of detoxification. J. Biol. Chem. 265:20715-29718, 1990.
3. See, for example: Dulik, D.M., Fenselau, C., Hilton, J. Characterization of melphalan-glutathione adducts whose formation is catalyzed by glutathione transferases. Biochem. Pharmacol. 35:3405-3409, 1986; Ciaccio, P.J., Tew, K.D., LaCreta, F.P. The spontaneous and glutathione S-transferase mediated reaction of chlorambucil with glutathione. Cancer Commun. 2:279-285, 1990; Armstrong, D.K., Gordon, G.B., Hilton, J., Streeper, R.T., Colvin, O.M., Davidson, N.E. Hepsulfam sensitivity in human breast cells: The role of glutathione and glutathione S-transferase in resistance. Cancer Res. 52:1416-1221, 1992.
4. See, for example: Dulik, D.M., Fenselau, C., Hilton, J. Characterization of melphalan-glutathione adducts whose formation is catalyzed by glutathione transferases. Biochem. Pharmacol. 35:3405-3409, 1986; Ciaccio, P.J., Tew, K.D., LaCreta, F.P. The spontaneous and glutathione S-transferase mediated reaction of chlorambucil with glutathione. Cancer Commun. 2:279-285, 1990; Armstrong, D.K., Gordon, G.B., Hilton, J., Streeper, R.T., Colvin, O.M., Davidson, N.E. Hepsulfam sensitivity in human breast cells: The role of glutathione and glutathione S-transferase in resistance. Cancer Res. 52:1416-1221, 1992.
5. See, for example: Dulik, D.M., Fenselau, C., Hilton, J. Characterization of melphalan-glutathione adducts whose formation is catalyzed by glutathione transferases. Biochem. Pharmacol. 35:3405-3409, 1986; Ciaccio, P.J., Tew, K.D., LaCreta, F.P. The spontaneous and glutathione S-transferase mediated reaction of chlorambucil with glutathione. Cancer Commun. 2:279-285, 1990; Armstrong, D.K., Gordon, G.B., Hilton, J., Streeper, R.T., Colvin, O.M., Davidson, N.E. Hepsulfam sensitivity in human breast cells: The role of glutathione and glutathione S-transferase in resistance. Cancer Res. 52:1416-1221, 1992.
6. Smith, M.T., Evans, C.G., Doane-Setzer, P., Castro, V.M., Tahir, M.K., Mannervik, B. Denitrosation of 1,3-bis-(2-chloroethyl)-1-nitrosourea by class mu glutathione transferases and its role in cellular resistance in rat brain tumor cells. Cancer Res. 49:2621-2625, 1989.
7. Tsuchida, S., Sato, K. Glutathione transferases and cancer. CRC Crit. Rev. Biochem. Mol. Biol. 27:337-384, 1992.
8. Mannervik, B., Awasthi, Y.C., Board, P.G., Hayes, J.D., Di Ilio, C., Ketterer, B., Listowsky, I., Morgenstern, R., Muramatsu, M., Pearson, W.R., Pickett, C.B., Sato, K., Widersten, M., Wolf, C.R. Nomenclature for human glutathione transferases. Biochem. J. 282:305-306, 1992.
9. Mannervik, B., Alin, P., Guthenberg, C., Jensson, H., Tahir, M. K., Warholm, M., Jornvall, H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206, 1985.
10. Meyer, D.J., Coles, B., Pemble, S.E., Gilmore, K.S., Fraser, G.M., Ketterer, B. Theta: A new class of glutathione transferase purified from rat and man. Biochem. J. 274:409-414, 1991.
11. Montali, J.A., Wheatley, J.B., Schmidt, D.E. Comparison of glutathione S-transferases in levels in predicting the efficacy of a novel alkylating agent. Cell. Pharm. 2:241-247, 1995.
12. Flatgaard, J., Bauer, K., Kauvar, L.M. Isozyme specificity of novel glutathione-S-transferase inhibitors. Cancer Chemother. Pharmacol. 33:63-70, 1993.
13. Lyttle, M.H., Hocker, M.D., Hui, H.C., Caldwell, C.G., Aaron, D.T., Engqvist-Goldstein, A., Flatgaard, J.E., Bauer, K.E. Isozyme-specific glutathione-S-transferase inhibitors: Design and synthesis. J. Med. Chem. 37:189-194, 1994.
14. Morgan, A.S., Ciaccio, P.J., Tew, K.D., Kauvar, L.M. Isozyme-specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human tumor cell lines. Cancer Chemother. Pharmacol. 37:363-370, 1996.
15. Bernstein, F., Koetzle, T.F., Willians, G.J.B., Meyer, E.F., Jr., Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T., Tasumi, M. The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 112:535-542, 1977.
16. Lineweaver, H., Burk, D.J. Am. Chem. Soc. 56:658-662, 1934.
17. Segel, I.H. "Enzymes in Biochemical Calculations." New York: Wiley, 1976:204-323.
18. Stenberg, G, Bjornestedt, R., Mannervik, B. Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line. Prot. Expr. Purif. 3:80-84, 1992.
19. Comstock, K.E., Widersten, M., Hao, X.-Y., Henner, W.D., Mannervik, B. A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human mu class enzymes. Arch. Biochem. Biophys. 311:487-495, 1994.
20. Kolm, R.H., Stenberg, G., Widersten, M., Mannervik, B. High-level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA. Prot. Expr. Purif. 6:265-271, 1995.
21. Reinemer, P., Dirr, H.W., Ladenstein, R., LoBello, M., Federici, G., Huber, R., Parker, M.W. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 angstroms. J. Mol. Biol. 227:214-226, 1992.
22. Sinning, I., Kleywegt, G.J., Cowan, S.W., Reinemer, P., Dirr, H.W., Huber, R., Gilliland, G.L., Armstrong, R.N., Xji, Board, P.G., Olin, B., Mannervik, B., Jones, T.A. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes. J. Mol. Biol. 232:192-212, 1993.
23. Raghunathan, S., Chandross, R.J., Kretsinger, R.H., Allison, T.J., Penington, C.J., Rule, G.S. Crystal structure of human class mu glutathione transferase GST M2-2: Effects of lattice packing on conformational heterogeneity. J. Mol. Biol. 338:815-832, 1994.
24. InsightII, Version 5.3. Biosym/MSI, San Diego, CA.
25. Viswanadhan, V.N., Ghose, A.K., Revankar, G.R., Robins, R.K. Atomic physicochemical parameters for three dimensional structure directed quantitative structure-activity relationships. 4. Additional parameters for hydrophobic and dispersive interactions and their application for an automated superposition of certain naturally occurring nucleoside antibiotics. J. Chem. Inf. Comput. Sci. 29:163-172, 1989.
26. Gaillard, P., Carrupt, P.-A., Testa, B., Boubon, A. Molecular lipophilicity potential, a tool in 3D QSAR: Method and applications. J. Comp.-Aid. Design 8:83-94, 1994
27. Ketterer, B., Meyer, D.J., Clark, A.G. Soluble glutathione transferase isozymes. In: "Glutathione Conjugation Mechanisms and Biological Significance." Sies, H., Ketterer, B. (eds.). New York: Academic Press, 1988:74-127.
28. Wilce, M.C.J., Parker, M.W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205:1-18, 1994.
29. Dirr, H., Reinemer, P., Huber, R. X-ray crystal structures of cytosolic glutathione S-transferases: Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:645-661, 1994.
30. PDB Release, Version 76, April 1996.
31. Cameron, A.D., Sinning, I., L'Hermite, G., Olin, B., Board, P.G., Mannervik, B., Jones, T.A. Structural analysis of human alpha-class glutathione transferase A1-1 in the Apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure 3:717-727, 1995.
32. Zeng, K., Rose, J., Chen, H., Strickland, C., Tu, C.D., Wang, B.C. A Surface Mutant (G82R) of a Human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins 20:259-263, 1994.
33. Ji, X., Zhang, P., Armstrong, R.N., Gilliland, G.L. The three-dimensional structure of a glutathione S-transferase from the mu gene class: Structural analysis of the binary complex of isoenzyme 3-3 and glutathione At 2.2-angstroms resolution. Biochemistry 31:10169-10184, 1992.
34. Ji, X., Sesay, M.A., Kickert, L., Prassad, S.M., Johnson, W.W., Ammon, H.L., Armstrong, R.N., Gilliland, G.L. Structure of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by x-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hvdroxy-9,10-dihydrophenanthrene. Biochemistry 33:1043-52, 1994.
35. Ji, X., Armstrong, R.N., Gilliland, G.L. Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry 32:12949-12954, 1993.
36. Garcia-Saez, I., Parraga, A., Phillips, M.F., Mantle, T.J., Coll, M. Molecular structure at 1.8 angstroms of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors. J. Mol. Biol. 237:298-314, 1994.
37. Ji, X., Von Rosenvinge, E.C., Johnson, W., Tomarev, S.I., Piatigorsky, J., Armstrong, R.N., Gilliland, G.L. Three-dimensional structure, catalytic properties and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens-crystallins of cephalopods. Biochemistry 34:5317-5328, 1995.
38. Lim, K., Ho, J.X., Keeling, K., Gilliland, G.L., Ji, X., Ruker, F., Carter, D.C. The three-dimensional structure of glutathione S-transferase of Schistosoma japonicum fused with a conserved neutralizing epitope on gp41 from HIV. Prot. Sci. 3:2233-2244, 1994.
39. Weinstein, H. Quantum chemical studies on molecular determinants for drug action. Ann. N.Y. Acad. Sci. 367:434-448, 1981.
40. Bone, R.G.A., Villar, H.O. Discriminating D1 and D2 agonists with a hydrophobic similarity index. J. Mol. Graphics 13:201-208, 1995.
41. Croizet, F., Langlois, M.H., Dubost, J.P., Braquet, P., Audry, E., Dallet, P., Colleter, J.C. Lipophilicity force field profile: An expressive visualization of the lipophilicity molecular potential gradient. J. Mol. Graphics 8:153-157, 1990.
42. Heiden, W., Moeckel, G., Brickmann, J. A new approach to analysis and display of local lipophilicity/hydrophilicity mapped on molecular surfaces. J. Comp.-Aid. Design 7:503-514, 1993.
43. Dougherty, D. A. Cation-π interactions in chemistry and biology: A new view of benzene. Phe, Tyr, and Trp. Science 271:163-168, 1996.
44. See, for example: Ringe, D. Binding by design. Nature 351:185-186, 1991; Klebe, G., Abraham, U. On the prediction of binding properties of drug molecules by comparative molecular field analysis. J. Med. Chem. 36:70-80, 1993; Mattos C., Rasmussen B., Ding X., Petsko G.A., Ringe D. Analogous inhibitors of elastase do not always bind analogously. Nat. Struct. Biol. 1:55-58, 1994.
45. See, for example: Ringe, D. Binding by design. Nature 351:185-186, 1991; Klebe, G., Abraham, U. On the prediction of binding properties of drug molecules by comparative molecular field analysis. J. Med. Chem. 36:70-80, 1993; Mattos C., Rasmussen B., Ding X., Petsko G.A., Ringe D. Analogous inhibitors of elastase do not always bind analogously. Nat. Struct. Biol. 1:55-58, 1994.
46. See, for example: Ringe, D. Binding by design. Nature 351:185-186, 1991; Klebe, G., Abraham, U. On the prediction of binding properties of drug molecules by comparative molecular field analysis. J. Med. Chem. 36:70-80, 1993; Mattos C., Rasmussen B., Ding X., Petsko G.A., Ringe D. Analogous inhibitors of elastase do not always bind analogously. Nat. Struct. Biol. 1:55-58, 1994.