메뉴 건너뛰기




Volumn 47, Issue 18, 2004, Pages 4530-4537

High-resolution structures of human aldose reductase holoenzyme in complex with stereoisomers of the potent inhibitor fidarestat: Stereospecific interaction between the enzyme and a cyclic imide type inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; CARBAMOYL GROUP; CITRIC ACID; CYSTEINE; FIDARESTAT; FUNCTIONAL GROUP; HISTIDINE; HOLOENZYME; IMIDE; MINALRESTAT; OXIDOREDUCTASE INHIBITOR; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 4143081343     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0497794     Document Type: Article
Times cited : (29)

References (33)
  • 1
    • 0032959371 scopus 로고    scopus 로고
    • Diabetes complications and their potential prevention: Aldose reductase inhibition and other approaches
    • Costantino, L.; Rastelli, G.; Vianello, P.; Cignarella, G.; Barlocco, D. Diabetes complications and their potential prevention: aldose reductase inhibition and other approaches. Med. Res. Rev. 1999, 19, 3-23.
    • (1999) Med. Res. Rev. , vol.19 , pp. 3-23
    • Costantino, L.1    Rastelli, G.2    Vianello, P.3    Cignarella, G.4    Barlocco, D.5
  • 2
    • 0031920049 scopus 로고    scopus 로고
    • Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications
    • Yabe-Nishimura, C. Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol. Rev. 1998, 50, 21-33.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 21-33
    • Yabe-Nishimura, C.1
  • 3
    • 0023913225 scopus 로고
    • The involvement of aldose reductase in diabetic complications
    • Kintoshita, J. H.; Nishimura, C. The involvement of aldose reductase in diabetic complications. Diabetes Metab. Res. 1988, 4, 323-337.
    • (1988) Diabetes Metab. Res. , vol.4 , pp. 323-337
    • Kintoshita, J.H.1    Nishimura, C.2
  • 4
    • 0033857113 scopus 로고    scopus 로고
    • Aldose reductase and the role of the polyol pathway in diabetic nephropathy
    • Dunlop, M. Aldose reductase and the role of the polyol pathway in diabetic nephropathy. Kidney Int. Suppl. 2000, 77, S3-S12.
    • (2000) Kidney Int. Suppl. , vol.77
    • Dunlop, M.1
  • 6
    • 0035684043 scopus 로고    scopus 로고
    • The role of aldose reductase inhibitors in diabetic complications: Recent trends
    • Kaul, C. L.; Ramarao, P. The role of aldose reductase inhibitors in diabetic complications: recent trends. Methods Find. Exp. Clin. Pharmacol. 2001, 23, 465-475.
    • (2001) Methods Find. Exp. Clin. Pharmacol. , vol.23 , pp. 465-475
    • Kaul, C.L.1    Ramarao, P.2
  • 7
    • 0036113742 scopus 로고    scopus 로고
    • Recent advances in aldose reductase inhibitors: Potential agents for the treatment of diabetic complications
    • Miyamoto, S. Recent advances in aldose reductase inhibitors: potential agents for the treatment of diabetic complications. Expert Opin. Ther. Pat. 2002, 12, 621-631.
    • (2002) Expert Opin. Ther. Pat. , vol.12 , pp. 621-631
    • Miyamoto, S.1
  • 8
    • 0032693720 scopus 로고    scopus 로고
    • Aldose reductase inhibitors: Therapeutic implications for diabetic complications
    • Oates, P. J.; Mylari, B. L. Aldose reductase inhibitors: therapeutic implications for diabetic complications. Exp. Opin. Invest. Drugs 1999, 8, 1-25.
    • (1999) Exp. Opin. Invest. Drugs , vol.8 , pp. 1-25
    • Oates, P.J.1    Mylari, B.L.2
  • 9
    • 0030931810 scopus 로고    scopus 로고
    • Aldose reductase inhibitors: The end of an era or the need for different trial design
    • Pfeifer, M. A.; Schumer, M. P.; Gelber D. A. Aldose reductase inhibitors: the end of an era or the need for different trial design. Diabetes 1997, 46, S82-S89.
    • (1997) Diabetes , vol.46
    • Pfeifer, M.A.1    Schumer, M.P.2    Gelber, D.A.3
  • 10
    • 2542643894 scopus 로고    scopus 로고
    • Ulta-high-resolution drug design II: Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat; implications for the binding of cyclic imide inhibitors
    • El-Kabbani, O.; Darmanin, C.; Schneider, T. R.; Hazemann, I.; Ruiz, F.; Oka, M.; Joachimiak, A.; Schulze-Briese, C.; Tomizaki, T.; Mitschler, A.; Podjarny, A. Ulta-high-resolution drug design II: Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat; implications for the binding of cyclic imide inhibitors. Proteins 2004, 55, 805-813.
    • (2004) Proteins , vol.55 , pp. 805-813
    • El-Kabbani, O.1    Darmanin, C.2    Schneider, T.R.3    Hazemann, I.4    Ruiz, F.5    Oka, M.6    Joachimiak, A.7    Schulze-Briese, C.8    Tomizaki, T.9    Mitschler, A.10    Podjarny, A.11
  • 11
    • 0036191826 scopus 로고    scopus 로고
    • Discovery of new inhibitors of aldose reductase from molecular docking and database screening
    • Rastelli, G.; Ferrari, A. M.; Costantino, L.; Gamverini, M. C. Discovery of new inhibitors of aldose reductase from molecular docking and database screening. Bioorg. Med. Chem. 2002, 10, 1437-1450.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1437-1450
    • Rastelli, G.1    Ferrari, A.M.2    Costantino, L.3    Gamverini, M.C.4
  • 12
    • 0032578366 scopus 로고    scopus 로고
    • Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites
    • El-Kabbani, O.; Wilson, D.; Petrash, J. M.; Quiocho, F. A. Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites. Mol. Vision 1998, 4, 19-25.
    • (1998) Mol. Vision , vol.4 , pp. 19-25
    • El-Kabbani, O.1    Wilson, D.2    Petrash, J.M.3    Quiocho, F.A.4
  • 13
    • 0031570301 scopus 로고    scopus 로고
    • 'Specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
    • Urzhumtsev, A.; Tête-Favier, F.; Mitschler, A.; Barbanton, J.; Barth, P.; Urzhumtseva, J. F.; Biellmann, A. D.; Podjarny, A.; Moras, D. A. 'Specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Structure 1997, 5, 601-612.
    • (1997) Structure , vol.5 , pp. 601-612
    • Urzhumtsev, A.1    Tête-Favier, F.2    Mitschler, A.3    Barbanton, J.4    Barth, P.5    Urzhumtseva, J.F.6    Biellmann, A.D.7    Podjarny, A.8    Moras, D.A.9
  • 14
    • 0033920645 scopus 로고    scopus 로고
    • A potent aldose reductase inhibitor, (2S,4S)-6-Fluoro-2′, 5′dioxyspiro[chroman-4,4′-imidazoline]-2-carboxamide (Fidarestat): Its absolute configuration and interaction with aldose reductase by X-ray crystallography
    • Oka, M.; Matsumoto, Y.; Sugiyama, S.; Tsuruta, N.; Matsushima, M. A potent aldose reductase inhibitor, (2S,4S)-6-Fluoro-2′, 5′dioxyspiro[chroman-4,4′-imidazoline]-2-carboxamide (Fidarestat): its absolute configuration and interaction with aldose reductase by X-ray crystallography. J. Med. Chem. 2000, 43, 2479-2483.
    • (2000) J. Med. Chem. , vol.43 , pp. 2479-2483
    • Oka, M.1    Matsumoto, Y.2    Sugiyama, S.3    Tsuruta, N.4    Matsushima, M.5
  • 16
    • 0027461303 scopus 로고
    • Molecular cloning of testicular 20 alpha-hydroxysteriod dehydrogenase: Identity with aldose reductase
    • Warren, J. C.; Murdock, G. L.; Ma, Y.; Goodman, S. R.; Zimmer, W. E. Molecular cloning of testicular 20 alpha-hydroxysteriod dehydrogenase: identity with aldose reductase. Biochemistry 1993, 32, 1401-1406.
    • (1993) Biochemistry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimmer, W.E.5
  • 17
    • 0001290630 scopus 로고
    • Molecular biology of aldose reductase
    • Tanimoto, T.; Nishijama, C. Molecular biology of aldose reductase. Exp. Med. 1991, 9, 541-547.
    • (1991) Exp. Med. , vol.9 , pp. 541-547
    • Tanimoto, T.1    Nishijama, C.2
  • 18
    • 0029039747 scopus 로고
    • Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase
    • Feather, M. S.; Flynn, T. G.; Munro, K. A.; Kubiseski, T. J.; Walton, D. J. Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim. Biophys. Acta 1995, 1244, 10-16.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 10-16
    • Feather, M.S.1    Flynn, T.G.2    Munro, K.A.3    Kubiseski, T.J.4    Walton, D.J.5
  • 19
    • 0030041937 scopus 로고    scopus 로고
    • Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: Aldose reductase, glyoxalase I, and glyoxalase II-a clinical research center study
    • Ratliff, D. M.; Van der Jagt, D. J.; Eaton, R. P.; Van der Jagt, D. L. Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II-a clinical research center study. J. Clin. Endocrinol. Metab. 1996, 81, 488-492.
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 488-492
    • Ratliff, D.M.1    Van Der Jagt, D.J.2    Eaton, R.P.3    Van Der Jagt, D.L.4
  • 20
    • 33947131757 scopus 로고    scopus 로고
    • Aldose and aldehyde reductases: Structure-function studies on the coenzyme and inhibitor-binding sites
    • El-Kabbani, O.; Old, S. E.; Ginell, S. L.; Carper, D. A. Aldose and aldehyde reductases: structure-function studies on the coenzyme and inhibitor-binding sites. Mol. Vision 1999, 5, 20-26.
    • (1999) Mol. Vision , vol.5 , pp. 20-26
    • El-Kabbani, O.1    Old, S.E.2    Ginell, S.L.3    Carper, D.A.4
  • 21
    • 0000243829 scopus 로고
    • PROCHECK a program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0028344047 scopus 로고
    • Synthesis and aldose reductase inhibitory activity of 2-substituted-6-fluora-2,3-dihydrospiro [4H-1-benzopyran-4,4′- imidazolidine]-2′, 5′-diones
    • Yamaguchi, T.; Miura, K.; Usui, T.; Unno, R.; Matsumoto, Y.; Fukushima, M.; Mizuno, K.; Kondo, Y.; Baba, Y.; Kurono, M. Synthesis and aldose reductase inhibitory activity of 2-substituted-6-fluora-2,3-dihydrospiro [4H-1-benzopyran-4,4′-imidazolidine]-2′, 5′-diones. Arzneim.-Forsch. /Drug Res. 1994, 44, 344-348.
    • (1994) Arzneim.-Forsch./Drug Res. , vol.44 , pp. 344-348
    • Yamaguchi, T.1    Miura, K.2    Usui, T.3    Unno, R.4    Matsumoto, Y.5    Fukushima, M.6    Mizuno, K.7    Kondo, Y.8    Baba, Y.9    Kurono, M.10
  • 24
    • 0024420222 scopus 로고
    • Cloning and sequence determination of human placental aldose reductase gene
    • Chung, S.; La Mendola, J. Cloning and sequence determination of human placental aldose reductase gene. J. Biol. Chem. 1989, 264, 4775-14777.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4775-14777
    • Chung, S.1    La Mendola, J.2
  • 25
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. Solvent content of protein crystals. J. Mol. Biol. 1968, 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A. T.; Krukowski, A.; Erickson, J. W. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A 1990, 46, 585-593.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 28
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL high-resolution refinement
    • Sheldrick, G.; Schneider, T. SHELXL: high-resolution refinement. Methods Enzymol. 1997, 277, 319-343.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.1    Schneider, T.2
  • 29
    • 0002908272 scopus 로고
    • TURBO-FRODO molecular graphics program
    • Silicon Graphics: Mountain View, CA
    • Roussel, A.; Cambillau, C. TURBO-FRODO molecular graphics program. In Silicon Graphics Geometry Partner Directory; Silicon Graphics: Mountain View, CA, 1989, pp 77-78.
    • (1989) Silicon Graphics Geometry Partner Directory , pp. 77-78
    • Roussel, A.1    Cambillau, C.2
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 1999, 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 31
    • 0035904883 scopus 로고    scopus 로고
    • Modelling studies of the active site of human sorbitol dehydrogenase: An approach to structure-based inhibitor design of the enzyme
    • Darmanin, C.; El-Kabbani, O. Modelling studies of the active site of human sorbitol dehydrogenase: an approach to structure-based inhibitor design of the enzyme. Bioorg. Med. Chem. Lett. 2001, 11, 3133-3136.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 3133-3136
    • Darmanin, C.1    El-Kabbani, O.2
  • 32
    • 0034658591 scopus 로고    scopus 로고
    • Modelling studies on the binding of substrate and inhibitor to the active site of human sorbitol dehydrogenase
    • Darmanin, C.; El-Kabbani, O. Modelling studies on the binding of substrate and inhibitor to the active site of human sorbitol dehydrogenase. Bioorg. Med. Chem. Lett. 2000, 10, 1101-1104.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1101-1104
    • Darmanin, C.1    El-Kabbani, O.2
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991, 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.