Docking and molecular dynamics studies at trypanothione reductase and glutathione reductase active sites

Journal of Molecular Modeling

Volumn 8, Issue 5, 2002, Pages 173-183

  Iribarne, Federico ^a   Paulino, Margot ^a   Aguilera, Sara ^b   Murphy, Miguel ^b   Tapia, Orlando ^c  

^a UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

^b UNIVERSIDAD CATÓLICA DEL NORTE   (Chile)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

Chagas' disease; Computer design; Molecular dynamics; Selective inhibitors; Theoretical docking

Indexed keywords

ANTIPROTOZOAL AGENT; CYSTEINE; ENZYME INHIBITOR; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; GLYCINE; NITROFURAN DERIVATIVE; SPERMIDINE; TRYPANOTHIONE; TRYPANOTHIONE REDUCTASE;

ANTIPROTOZOAL ACTIVITY; ARTICLE; BINDING AFFINITY; CHAGAS DISEASE; COMPUTER SIMULATION; CONTROLLED STUDY; CORRELATION FUNCTION; DRUG DESIGN; DRUG STRUCTURE; DRUG SYNTHESIS; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; THEORETICAL STUDY; TRYPANOSOMA CRUZI; VALIDATION PROCESS;

BINDING SITES; COMPUTER SIMULATION; ELECTROSTATICS; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; LIGANDS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; NADH, NADPH OXIDOREDUCTASES; SOLVENTS; SPERMIDINE;

TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0036973882     PISSN: 16102940     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00894-002-0082-0     Document Type: Article

References (49)

1. Moncayo A (1993) In: Tropical disease research; progress 1991-1992. World Health Organization, Geneva, pp 67-72
2. deCastro S (1993) Acta Trop 53:83-98
3. Schirmer RH, Muller JG, Krauth-Siegel RL (1995) Angew Chem Int Ed Engl 34:141-154
4. Verlinde CLMJ (1994) Structure 2:577-587
5. Hunter WN, Bailey S, Habash J, Harrop SJ, Helliwell JR, Aboagye-Kwarteng T, Smith K, Fairlamb AH (1992) J Mol Biol 227:322-333
6. Fairlamb AH (1999) Medicina 59:179-187
7. Fairlamb AH, Cerami A (1992) Annu Rev Microbiol 46:695-729
8. Karplus PA, Schulz GE (1989) J Mol Biol 210:163-180
9. Mittl PRE, Schulz GE (1994) Protein Sci 3:799-809
10. Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL (1994) Proteins 18:161-173
11. Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN (1996) Protein Sci 5:52-61
12. Bailey S, Smith K, Fairlamb AH, Hunter WN (1993) Eur J Biochem 213:67-75
13. Bond CS, Zhang Y, Berriman M, Cunningham ML, Fairlamb AH, Hunter WN (1999) Structure 7:81-89
14. Shames SL, Fairlamb AH, Cerami A, Walsh CT (1986) Biochemistry 25:3519-3526
15. Krauth-Siegel RL, Enders B, Henderson GB, Fairlamb AH, Schirmer RH (1987) Eur J Biochem 164:123-128
16. Ghisla SK, Massey V (1989) Eur J Biochem 181:1-17
17. Schirmer RH, Krauth-Siegel RL, Schulz GE (1989) In: Dolphin P, Poulson R, Avramovic O (eds) Glutathione: chemical, biochemical and medical aspects, part A. Wiley, New York, pp 553-596
18. Hunter WN, Smith K, Derewenda Z, Harrop SJ, Habash J, Islam MS, Helliwell JR., Fairlamb AH (1990) J Mol Biol 216:235-237
19. Karplus PA, Pai EF, Schulz GE (1989) Eur J Biochem 178:693-703
20. Diaz W, Aullo JM, Paulino M, Tapia O (1996) Chem Phys 204:195-203
21. Iribarne F, Paulino M, Tapia O (2000) Theor Chem Acc 103:451-462
22. Henderson GB, Fairlamb AH, Ulrich P, Cerami A (1987) Biochemistry 26:3023-3027
23. Dumas C, Ouelette M, Tovar J, Cunningham ML, Fairlamb AH, Tamar S, Olivier M, Papadopoulou B (1997) EMBO J 16:2590-2598
24. Tovar J, Cunningham ML, Smith AC, Croft SL, Fairlamb AH (1998) Proc Natl Acad Sci USA 95:5311-5316
25. Tovar J, Wilkinson S, Mottram JC, Fairlamb AH (1998) Mol Microbiol 29:653-660
26. Henderson GB, Ulrich P, Fairlamb AH, Rosenberg I, Pereira M, Sela M, Cerami A (1988) Proc Natl Acad Sci USA 85:5374-5378
27. Jockers-Scherubl MC, Schirmer RH, Krauth-Siegel LR (1989) Eur J Biochem 180:267-272
28. Mester B, Hikichi N, Hansz M, Paulino M (1990) Chromatographia 30:191-194
29. Benson TJ, McKie JH, Garforth J, Borges A, Fairlamb AH, Douglas KT (1992) Biochem J 286:9-11
30. Cunningham ML, Zvelebil MJJM, Fairlamb AH (1994) Eur J Biochem 221:285-295
31. Jacoby EM, Schlichting I, Lantwin CB, Kabsch W, Krauth-Siegel RL (1996) PROTEINS 24:73-80
32. Chan C, Yin H, Garforth J, McKie JH, Jaouhari R, Speers P, Douglas KT, Rock PJ, Yardley V, Croft SL, Fairlamb AH (1998) J Med Chem 41:148-156
33. Stoppani AOM (1999) Medicina 59:147-165
34. Tapia O, Paulino M, Stamato FMLG (1994) Mol Eng 3:377-414
35. Kuntz ID (1992) Science 257:1078-1082
36. Kuntz ID, Meng EC, Shoichet BK (1994) Acc Chem Res 27:117-123
37. Jones TA, Kjeldgaard M (1990) Manual for O. Uppsala University
38. van Gunsteren WF, Berendsen HJC (1987) Groningen Molecular Simulation (GROMOS) Library Manual. Biomos, Groningen, The Netherlands
39. Berendsen HJC, Postma JPM, Di Nola A, van Gunsteren WF, Haak HR (1984) J Chem Phys 81:3684-3690
40. Åqvist J, Hansson T (1996) J Phys Chem 100:9512-9521
41. Cerecetto H, Di Maio R, Ibarruri G, Seoane G, Denicola A, Quijano C, Peluffo G, Paulino M (1998) Il Farmaco 53:89-94
42. Nilsson O (1990) J Mol Graph 8:192-200
43. Nicholls A, Sharp K, Honig B (1991) PROTEINS 11:281-296
44. Marsh I, Bradley M (1997) Eur J Biochem 248:690-694
45. Faerman CH, Savvide SN, Strickland C, Breidenbach MA, Ponasik JA, Ganem B, Ripoll D, Krauth-Siegel KL, Karplus PA (1996) Bioorg Med Chem 4:1247-1253
46. Paulino M., Iribarne F, Hans M, Vega M, Seoane G, Cerecetto H, Di Maio R, Caracelli I, Zukerman-Schpector J, Olea C, Stoppani AOM, Berriman M, Fairlamb AH, Tapia O (2002) J Mol Struct (Theochem) in press
47. Meng EC, Shoichet BK, Kuntz ID (1992) J Comput Chem 13:505-524
48. Meng EC, Gschwend DA, Blaney JM, Kuntz ID (1993) PROTEINS 17:266-278
49. Kenney JF, Keeping ES (1962) The standard deviation. In: Mathematics of statistics Pt. 1, 3rd edn. Van Nostrand, Princeton, N.J., pp 77-80