메뉴 건너뛰기




Volumn 7, Issue 9, 1999, Pages 1067-1078

Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue

Author keywords

Binuclear zinc site; Crystal structure; Glutathione; Glyoxalase II; Thiolesterase

Indexed keywords

GLUTATHIONE DERIVATIVE; HYDROXYACYLGLUTATHIONE HYDROLASE; THIOESTER;

EID: 0033200323     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80174-9     Document Type: Article
Times cited : (164)

References (57)
  • 1
    • 0000118223 scopus 로고
    • Glyoxalase I
    • Jakoby, W. B., ed. Academic Press, New York
    • 1. Mannervik, B. (1980). Glyoxalase I. In Enzymatic Basis of Detoxication (Jakoby, W. B., ed.), Vol. 2, pp. 263-273. Academic Press, New York.
    • (1980) Enzymatic Basis of Detoxication , vol.2 , pp. 263-273
    • Mannervik, B.1
  • 2
    • 0025298551 scopus 로고
    • The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life
    • 2. Thornalley, P.J. (1990). The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269, 1-11.
    • (1990) Biochem. J. , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 3
    • 0025787465 scopus 로고
    • Kinetic parameters for the elimination reaction catalysed by triosephosphate isomerase and an estimation of the reaction's physiological significance
    • 3. Richard, J.P. (1991). Kinetic parameters for the elimination reaction catalysed by triosephosphate isomerase and an estimation of the reaction's physiological significance. Biochemistry 30, 4581-4585.
    • (1991) Biochemistry , vol.30 , pp. 4581-4585
    • Richard, J.P.1
  • 4
    • 0031590782 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a rat spermatogenesis-associated protein RSP29
    • 4. Ji, X., Moore, H.D., Russell, R.G. & Watts, D.J. (1997). cDNA cloning and characterization of a rat spermatogenesis-associated protein RSP29. Biochem. Biophys. Res. Commun. 241, 714-719.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 714-719
    • Ji, X.1    Moore, H.D.2    Russell, R.G.3    Watts, D.J.4
  • 5
    • 0027454552 scopus 로고
    • The glyoxalase system in health and disease
    • 5. Thornalley, P. J. (1993). The glyoxalase system in health and disease. Mol. Aspects. Med. 14, 287-371.
    • (1993) Mol. Aspects. Med. , vol.14 , pp. 287-371
    • Thornalley, P.J.1
  • 6
    • 0028038969 scopus 로고
    • Antimalarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester
    • 6. Thornalley, P.J., Strath, M. & Wilson, R.J. (1994). Antimalarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester. Biochem. Pharmacol. 47, 418-420.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 418-420
    • Thornalley, P.J.1    Strath, M.2    Wilson, R.J.3
  • 7
    • 0014665769 scopus 로고
    • Glyoxalase inhibitors as potential anticancer agents
    • 7. Vince, R. & Wadd, W.B. (1969). Glyoxalase inhibitors as potential anticancer agents. Biochem. Biophys. Res. Commun. 34, 593-598.
    • (1969) Biochem. Biophys. Res. Commun. , vol.34 , pp. 593-598
    • Vince, R.1    Wadd, W.B.2
  • 8
    • 0026465674 scopus 로고
    • Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy
    • 8. Hamilton, D.S. & Creighton, D.J. (1992). Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy. J. Biol. Chem. 267, 24933-24936.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24933-24936
    • Hamilton, D.S.1    Creighton, D.J.2
  • 9
    • 4244040278 scopus 로고    scopus 로고
    • Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: Involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors
    • 9. Thornalley, P.J. (1998). Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors. Chem. Biol. Interact. 111-112, 137-151.
    • (1998) Chem. Biol. Interact. , vol.111-112 , pp. 137-151
    • Thornalley, P.J.1
  • 10
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I - Evidence for gene duplication and 3D domain swapping
    • 10. Cameron, A.D., Olin, B., Ridderström, M., Mannervik, B. & Jones, T.A. (1997). Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. EMBO J. 16, 3386-3395.
    • (1997) EMBO J. , vol.16 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderström, M.3    Mannervik, B.4    Jones, T.A.5
  • 11
    • 0015791813 scopus 로고
    • Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver
    • 11. Uotila, L. (1973). Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12, 3944-3951.
    • (1973) Biochemistry , vol.12 , pp. 3944-3951
    • Uotila, L.1
  • 13
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • 13. Neuwald, A.F., Liu, J.S., Lipman, D.J. & Lawrence, C.E. (1997). Extracting protein alignment models from the sequence database. Nucleic Acids Res. 25, 1665-1677.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1665-1677
    • Neuwald, A.F.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 14
    • 0031728459 scopus 로고    scopus 로고
    • A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases
    • 14. Melino, S., Capo, C., Dragani, B., Aceto, A. & Petruzzelli, R. (1998). A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases. Trends Biochem. Sci. 23, 381-382.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 381-382
    • Melino, S.1    Capo, C.2    Dragani, B.3    Aceto, A.4    Petruzzelli, R.5
  • 15
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold
    • 15. Carfi, A., et al. & Dideberg, O. (1995). The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14, 4914-4921.
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1    Dideberg, O.2
  • 16
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis
    • 16. Concha, N.O., Rasmussen, B.A., Bush, K. & Herzberg, O. (1996). Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure 4, 823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 17
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution
    • 17. Ullah, J.H., et al. & Spencer, J. (1998). The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J. Mol. Biol. 284, 125-136.
    • (1998) J. Mol. Biol. , vol.284 , pp. 125-136
    • Ullah, J.H.1    Spencer, J.2
  • 18
    • 0030608678 scopus 로고    scopus 로고
    • Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity
    • 18. Crowder, M.W., Maiti, M.K., Banovic, L. & Makaroff, C.A. (1997). Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity. FEBS Lett. 418, 351-354.
    • (1997) FEBS Lett. , vol.418 , pp. 351-354
    • Crowder, M.W.1    Maiti, M.K.2    Banovic, L.3    Makaroff, C.A.4
  • 19
    • 0028237443 scopus 로고
    • S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II
    • 19. Murthy, N.S., Bakeris, T., Kavarana, M.J., Hamilton, D.S., Lan, Y. & Creighton, D.J. (1994). S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II. J. Med. Chem. 37, 2161-2166.
    • (1994) J. Med. Chem. , vol.37 , pp. 2161-2166
    • Murthy, N.S.1    Bakeris, T.2    Kavarana, M.J.3    Hamilton, D.S.4    Lan, Y.5    Creighton, D.J.6
  • 20
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • 20. Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 21
    • 0031924109 scopus 로고    scopus 로고
    • Structural characterization of human glyoxalase II as probed by limited proteolysis
    • 21. Aceto, A., et al. & Petruzzelli, R. (1998). Structural characterization of human glyoxalase II as probed by limited proteolysis. Biochem. Mol. Biol. Int. 44, 761-769.
    • (1998) Biochem. Mol. Biol. Int. , vol.44 , pp. 761-769
    • Aceto, A.1    Petruzzelli, R.2
  • 22
    • 0031887008 scopus 로고    scopus 로고
    • X-ray structure of the Znll beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form
    • 22. Carfi, A., Duée, E., Paul-Soto, R., Galleni, M., Frère, J.M. & Dideberg, O. (1998). X-ray structure of the Znll beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form. Acta Crystallogr. D 54, 45-57.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 45-57
    • Carfi, A.1    Duée, E.2    Paul-Soto, R.3    Galleni, M.4    Frère, J.M.5    Dideberg, O.6
  • 23
    • 0026409452 scopus 로고
    • Structural biology of zinc
    • 23. Christianson, D.W. (1991). Structural biology of zinc. Adv. Prot. Chem. 42, 281-355.
    • (1991) Adv. Prot. Chem. , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 24
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • 24. Alberts, I.L., Nadassy, K. & Wodak, S.J. (1998). Analysis of zinc binding sites in protein crystal structures. Prot. Sci. 7, 1700-1716.
    • (1998) Prot. Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 25
    • 0027303379 scopus 로고
    • New perspectives on zinc biochemistry: Cocatalytic sites in multi-zinc enzymes
    • 25. Vallee, B.L. & Auld, D.S. (1993). New perspectives on zinc biochemistry: cocatalytic sites in multi-zinc enzymes. Biochemistry 32, 6493-6500.
    • (1993) Biochemistry , vol.32 , pp. 6493-6500
    • Vallee, B.L.1    Auld, D.S.2
  • 26
    • 0029116127 scopus 로고
    • Transition state analogue L-leucinephosphonic acid bound to bovine lens aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form
    • 26. Sträter, N. & Lipscomb, W.N. (1995). Transition state analogue L-leucinephosphonic acid bound to bovine lens aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form. Biochemistry 34, 9200-9210.
    • (1995) Biochemistry , vol.34 , pp. 9200-9210
    • Sträter, N.1    Lipscomb, W.N.2
  • 27
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid-phosphatase containing a dinuclear Fe(III)-Zn(II) active-site
    • 27. Sträter, N., Klabunde, T., Tucker, P., Witzel, H. & Krebs, B. (1995). Crystal structure of a purple acid-phosphatase containing a dinuclear Fe(III)-Zn(II) active-site. Science 268, 1489-1492.
    • (1995) Science , vol.268 , pp. 1489-1492
    • Sträter, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 28
    • 0031833739 scopus 로고    scopus 로고
    • 1.85 Å resolution structure of the zinc (II) beta-lactamase from Bacillus cereus
    • 28. Carfi, A., Duée, E., Galleni, M., Frère, J.M. & Dideberg, O. (1998). 1.85 Å resolution structure of the zinc (II) beta-lactamase from Bacillus cereus. Acta Crystallogr. D 54, 313-323.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 313-323
    • Carfi, A.1    Duée, E.2    Galleni, M.3    Frère, J.M.4    Dideberg, O.5
  • 29
    • 0032497362 scopus 로고    scopus 로고
    • Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 Å resolution: Binuclear active site with features of a mononuclear enzyme
    • 29. Fabiane, S.M., Sohi, M.K., Wan, T., Payne, D.J., Bateson, J.H., Mitchell, T. & Sutton, B.J. (1998). Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 Å resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry 37, 12404-12411.
    • (1998) Biochemistry , vol.37 , pp. 12404-12411
    • Fabiane, S.M.1    Sohi, M.K.2    Wan, T.3    Payne, D.J.4    Bateson, J.H.5    Mitchell, T.6    Sutton, B.J.7
  • 30
    • 0022446565 scopus 로고
    • Inhibition by glutathione derivatives of bovine liver glyoxalase II (hydroxyacylglutathione hydrolase) as a probe of the N- and S-sites for substrate binding
    • 30. Al-Timari, A. & Douglas, K.T. (1986). Inhibition by glutathione derivatives of bovine liver glyoxalase II (hydroxyacylglutathione hydrolase) as a probe of the N- and S-sites for substrate binding. Biochim. Biophys. Acta 870, 219-225.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 219-225
    • Al-Timari, A.1    Douglas, K.T.2
  • 31
    • 0033550054 scopus 로고    scopus 로고
    • The reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue
    • in press
    • 31. Cameron, A.D., Ridderström, M., Olin, B., Kavarana, M.J., Creighton, D.J. & Mannervik, B. (1999). The reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry 38, in press.
    • (1999) Biochemistry , vol.38
    • Cameron, A.D.1    Ridderström, M.2    Olin, B.3    Kavarana, M.J.4    Creighton, D.J.5    Mannervik, B.6
  • 32
    • 0019883186 scopus 로고
    • S-2-hydroxyacylglutathione hydrolase (glyoxalase II): Active-site mapping of a nonserine thiolesterase
    • 32. Ball, J.C. & Vander Jagt, D.L. (1981 ). S-2-hydroxyacylglutathione hydrolase (glyoxalase II): active-site mapping of a nonserine thiolesterase. Biochemistry 20, 899-905.
    • (1981) Biochemistry , vol.20 , pp. 899-905
    • Ball, J.C.1    Vander Jagt, D.L.2
  • 33
    • 0027256148 scopus 로고
    • Glyoxalase II: Molecular characteristics, kinetics and mechanism
    • 33. Vander Jagt, D.L. (1993). Glyoxalase II: molecular characteristics, kinetics and mechanism. Biochem. Soc. Trans. 21, 522-527.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 522-527
    • Vander Jagt, D.L.1
  • 34
    • 0032510815 scopus 로고    scopus 로고
    • Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): A crystallographic study at 1.85 Å resolution
    • 34. Fitzgerald, P.M., Wu, J.K. & Toney, J.H. (1998). Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85 Å resolution. Biochemistry 37, 6791-6800.
    • (1998) Biochemistry , vol.37 , pp. 6791-6800
    • Fitzgerald, P.M.1    Wu, J.K.2    Toney, J.H.3
  • 36
    • 0030761248 scopus 로고    scopus 로고
    • Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins
    • 36. Bito, A., Haider, M., Hadler, I. & Breitenbach, M. (1997). Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins. J. Biol. Chem. 272, 21509-21519.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21509-21519
    • Bito, A.1    Haider, M.2    Hadler, I.3    Breitenbach, M.4
  • 37
    • 0027968068 scopus 로고
    • ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 37. Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994). ClustalW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0031282507 scopus 로고    scopus 로고
    • Molecular characterization of glyoxalase II from Arabidopsis thaliana
    • 38. Maiti, M.K., Krishnasamy, S., Owen, H.A. & Makaroff, C.A. (1997). Molecular characterization of glyoxalase II from Arabidopsis thaliana. Plant Mol. Biol. 35, 471-481.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 471-481
    • Maiti, M.K.1    Krishnasamy, S.2    Owen, H.A.3    Makaroff, C.A.4
  • 39
    • 0024207748 scopus 로고
    • Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes
    • 39. Guha, M.K., Vander Jagt, D.L. & Creighton, D.J. (1988). Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes. Biochemistry 27, 8818-8822.
    • (1988) Biochemistry , vol.27 , pp. 8818-8822
    • Guha, M.K.1    Vander Jagt, D.L.2    Creighton, D.J.3
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • 40. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276A, 307-326.
    • (1997) Methods Enzymol. , vol.276 A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 41. Collaborative Computation Project Number 4. (1994). The CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 42
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • 42. de La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276A, 472-494.
    • (1997) Methods Enzymol. , vol.276 A , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 44
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • 44. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 45
    • 0030841587 scopus 로고    scopus 로고
    • Electron density map interpretation
    • 45. Jones, T.A. & Kjeldgaard, M.O. (1997). Electron density map interpretation. Methods Enzymol. 277, 173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.O.2
  • 46
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software system for macromolecular structure determination
    • 46. Brünger, A.T., et al. & Warren, G.L. (1998). Crystallography and NMR system: a new software system for macromolecular structure determination. Acta Cryst. D 54, 905-921.
    • (1998) Acta Cryst. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 47
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • 47. Brünger, A.T. & Krukowski, A. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A 46, 585-593.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2
  • 48
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • 48. Rice, L.M. & Brünger, A.T. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 49
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 49. Murshodov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta. Crystallogr. D 53, 240-255.
    • (1997) Acta. Crystallogr. D , vol.53 , pp. 240-255
    • Murshodov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 50
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • 50. Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Crystallogr. D 49, 129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 51
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • 51. Engh, R.A. & Huber, R. (1992). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400.
    • (1992) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 52
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • 52. Kleywegt, G.J. & Jones, T.A. (1996). Phi/Psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 54
    • 0026244229 scopus 로고
    • MolScript: A program to produce both detailed and schematic plots of protein structures
    • 54. Kraulis, P.J. (1991 ). MolScript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 55
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • 55. Merrit, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta. Crystallogr. D 50, 869-873.
    • (1994) Acta. Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 56
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • 56. Wallace, A., Laskowski, R. & Thornton, J. (1995). LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.1    Laskowski, R.2    Thornton, J.3
  • 57
    • 0027412196 scopus 로고
    • ALSCRIPT a tool to format multiple sequence alignments
    • 57. Barton, G. J. (1993). ALSCRIPT a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.