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Volumn 5, Issue 6, 1997, Pages 751-761

Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design

Author keywords

Drug design; Malaria; Plasmodiurn falciparum; Triosephosphate isomerase; barrel

Indexed keywords

ANIMALIA; ESCHERICHIA COLI; PLASMODIUM FALCIPARUM;

EID: 0031570683     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00230-X     Document Type: Article
Times cited : (134)

References (52)
  • 1
    • 0018633747 scopus 로고
    • Biochemistry of Plasmodium (malarial parasites)
    • Sherman, I.W. (1979). Biochemistry of Plasmodium (malarial parasites). Microbiol. Rev. 43, 453-495.
    • (1979) Microbiol. Rev. , vol.43 , pp. 453-495
    • Sherman, I.W.1
  • 2
    • 0023908225 scopus 로고
    • The use of enzymopathic human red cells in study of malarial parasite glucose metabolism
    • Roth, E., et al., & Rosa, R. (1988). The use of enzymopathic human red cells in study of malarial parasite glucose metabolism. Blood 71, 1408-1413.
    • (1988) Blood , vol.71 , pp. 1408-1413
    • Roth, E.1    Rosa, R.2
  • 3
    • 0022881599 scopus 로고
    • Dynamic interactions of enzymes involved in triosephosphate metabolism
    • Orosz, F. & Ovadi, J. (1986). Dynamic interactions of enzymes involved in triosephosphate metabolism. Eur. J. Biochem. 160, 615-619.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 615-619
    • Orosz, F.1    Ovadi, J.2
  • 4
    • 0025763437 scopus 로고
    • Enzyme catalysis: Not different, just better
    • Knowles, J.R. (1991). Enzyme catalysis: not different, just better. Nature 350, 121-124.
    • (1991) Nature , vol.350 , pp. 121-124
    • Knowles, J.R.1
  • 5
    • 0027488866 scopus 로고
    • Prolonged hemolytic anemia in malaria and autoantibodies against triosephosphate isomerase
    • Ritter, K., Kuhlencord, A., Thomssen, R. & Bommer, W. (1993). Prolonged hemolytic anemia in malaria and autoantibodies against triosephosphate isomerase. Lancet 342, 1333-1334.
    • (1993) Lancet , vol.342 , pp. 1333-1334
    • Ritter, K.1    Kuhlencord, A.2    Thomssen, R.3    Bommer, W.4
  • 6
    • 0026531647 scopus 로고
    • A protective monoclonal antibody specifically recognizes and alters the catalytic activity of triosephosphate isomerase
    • Harn, D.A., Gu, W., Oligono, D.L., Mitsuyama, M., Gebremichael, A. & Ritcher, D. (1992). A protective monoclonal antibody specifically recognizes and alters the catalytic activity of triosephosphate isomerase. J. Immunol. 148, 562-571.
    • (1992) J. Immunol. , vol.148 , pp. 562-571
    • Harn, D.A.1    Gu, W.2    Oligono, D.L.3    Mitsuyama, M.4    Gebremichael, A.5    Ritcher, D.6
  • 7
    • 0027428306 scopus 로고
    • Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli
    • Ranie, J., Kumar, V.P. & Balaram, H. (1993). Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli. Mol. Biochem. Parasitol. 61, 159-170.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 159-170
    • Ranie, J.1    Kumar, V.P.2    Balaram, H.3
  • 8
    • 0026277508 scopus 로고
    • Is Plasmodium falciparum aldolase useful for rational drug design?
    • Dobeli, H., Itin, C., Meier, B. & Certa, U. (1991). Is Plasmodium falciparum aldolase useful for rational drug design? Acta Leiden 60, 135-140.
    • (1991) Acta Leiden , vol.60 , pp. 135-140
    • Dobeli, H.1    Itin, C.2    Meier, B.3    Certa, U.4
  • 9
    • 0030294274 scopus 로고    scopus 로고
    • The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design
    • Dunn, C.R., et al., & Holbrook., J.J. (1996). The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design. Nat. Struct. Biol. 3, 912-915.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 912-915
    • Dunn, C.R.1    Holbrook, J.J.2
  • 10
    • 0029137828 scopus 로고
    • The structure and evolution of α/β barrel proteins
    • Reardon, D. & Farber, G.K. (1995). The structure and evolution of α/β barrel proteins. FASEB J. 9, 497-503.
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 11
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 12
    • 0026779802 scopus 로고
    • Segmental movement: Definition of the structural requirement for loop closure in catalysis by triosephosphate isomerase
    • Sampson, N.S. & Knowles, J.R. (1992). Segmental movement: definition of the structural requirement for loop closure in catalysis by triosephosphate isomerase. Biochemistry 31, 8482-8487.
    • (1992) Biochemistry , vol.31 , pp. 8482-8487
    • Sampson, N.S.1    Knowles, J.R.2
  • 13
    • 0027242141 scopus 로고
    • Structure of the Open' and 'closed' state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
    • Noble, M.E.M, Zeelen, J. Ph. & Wierenga, R.K. (1993). Structure of the Open' and 'closed' state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism. Proteins 16, 311-326.
    • (1993) Proteins , vol.16 , pp. 311-326
    • Noble, M.E.M.1    Zeelen, J.Ph.2    Wierenga, R.K.3
  • 14
    • 0021112509 scopus 로고
    • Codon usage and mistranslation. in vivo basal level misreading of the MS2 coat protein message
    • Parker, J., Johnston, T.C., Borgia, P.T., Holtz, G., Remaut, E. & Fiers, W. (1983). Codon usage and mistranslation. In vivo basal level misreading of the MS2 coat protein message. J. Biol. Chem. 258, 10007-10012.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10007-10012
    • Parker, J.1    Johnston, T.C.2    Borgia, P.T.3    Holtz, G.4    Remaut, E.5    Fiers, W.6
  • 15
    • 0025785056 scopus 로고
    • Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M ammonium sulphate
    • Wierenga, R.K., Noble, M.E.M., Vriend, G., Nauche, S. & Hol, W.G.J. (1991). Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M ammonium sulphate. J. Mol. Biol. 220, 995-1015.
    • (1991) J. Mol. Biol. , vol.220 , pp. 995-1015
    • Wierenga, R.K.1    Noble, M.E.M.2    Vriend, G.3    Nauche, S.4    Hol, W.G.J.5
  • 18
    • 0000400122 scopus 로고
    • Structure of triosephosphate isomerase from E. coli determined at 2.6 Å resolution
    • Noble, M.E.M, Zeelen, J.Ph. & Wierenga, R.K. (1993). Structure of triosephosphate isomerase from E. coli determined at 2.6 Å resolution. Acta Cryst. D 49, 403-417.
    • (1993) Acta Cryst. D , vol.49 , pp. 403-417
    • Noble, M.E.M.1    Zeelen, J.Ph.2    Wierenga, R.K.3
  • 19
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interaction
    • Delboni, L.F., et al., & Hol, W.G.J. (1995). Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interaction. Protein Sci. 4, 2594-2604.
    • (1995) Protein Sci. , vol.4 , pp. 2594-2604
    • Delboni, L.F.1    Hol, W.G.J.2
  • 20
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase related human genetic disorders and comparison with the trypanosomal enzyme
    • Mande, S.C., Mainfroid, V., Kalk, K.H., Goraj, K., Martial, J.A. & Hol, W.G.J. (1994). Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 3, 810-821.
    • (1994) Protein Sci. , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfroid, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.J.6
  • 21
    • 0029916524 scopus 로고    scopus 로고
    • Three hTIM mutants that provide new insights on why TIM is a dimer
    • Mainfroid, V., et al., & Goraj, K. (1996). Three hTIM mutants that provide new insights on why TIM is a dimer. J. Mol. Biol. 257, 441-456.
    • (1996) J. Mol. Biol. , vol.257 , pp. 441-456
    • Mainfroid, V.1    Goraj, K.2
  • 22
    • 0026681342 scopus 로고
    • Crystallographic binding studies with triosephosphate isomerase: Conformational changes induced by substrate and substrate-analogues
    • Wierenga, R.K., Borchert, T.V. & Noble, M.E.M. (1992). Crystallographic binding studies with triosephosphate isomerase: conformational changes induced by substrate and substrate-analogues. FEBS Lett. 307, 34-39.
    • (1992) FEBS Lett. , vol.307 , pp. 34-39
    • Wierenga, R.K.1    Borchert, T.V.2    Noble, M.E.M.3
  • 23
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams, J.C. & McDermott, A.E. (1995). Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34, 8309-8319.
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 24
    • 0027081843 scopus 로고
    • Structure of the complex between triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: Binding at the active site despite an 'Open' flexible loop
    • Verlinde, C.L.M.J., et al., & Opperdoes, F.R. (1992). Structure of the complex between triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an 'Open' flexible loop. Protein Sci. 1, 1578-1584.
    • (1992) Protein Sci. , vol.1 , pp. 1578-1584
    • Verlinde, C.L.M.J.1    Opperdoes, F.R.2
  • 25
    • 0023069554 scopus 로고
    • Common elements on the surface of glycolytic enzymes from Trypanosoma brucei may serve as topogenic signals for import into glycosomes
    • Wierenga, R.K., et al., & Hol, W.G.J. (1987). Common elements on the surface of glycolytic enzymes from Trypanosoma brucei may serve as topogenic signals for import into glycosomes. EMBO J. 6, 215-221.
    • (1987) EMBO J. , vol.6 , pp. 215-221
    • Wierenga, R.K.1    Hol, W.G.J.2
  • 26
    • 0028090513 scopus 로고
    • Protein crystallography and infectious diseases
    • Verlinde, C.L.M.J., et al., & Hol, W.G.J. (1994). Protein crystallography and infectious diseases. Protein Sci. 3, 1670-1686.
    • (1994) Protein Sci. , vol.3 , pp. 1670-1686
    • Verlinde, C.L.M.J.1    Hol, W.G.J.2
  • 27
    • 0025282144 scopus 로고
    • Expression, purification, biochemical characterization and inhibition of recombinant Plasmodium falciparum aldolase
    • Dobeli, H., et al., & Certa U. (1990). Expression, purification, biochemical characterization and inhibition of recombinant Plasmodium falciparum aldolase. Mol. Biochem. Parasitol. 41, 259-268.
    • (1990) Mol. Biochem. Parasitol. , vol.41 , pp. 259-268
    • Dobeli, H.1    Certa, U.2
  • 28
    • 0029863567 scopus 로고    scopus 로고
    • Inhibition and catalytic mechanism of HIV-1 aspartic protease
    • Silva, A.M., Cachau, R.E., Sham, H.L. & Erickson, J.W. (1996). Inhibition and catalytic mechanism of HIV-1 aspartic protease. J. Mol. Biol. 255, 321-346.
    • (1996) J. Mol. Biol. , vol.255 , pp. 321-346
    • Silva, A.M.1    Cachau, R.E.2    Sham, H.L.3    Erickson, J.W.4
  • 29
    • 0001637467 scopus 로고
    • Formation and reaction of sulfenic acids in proteins
    • Allison, W.S. (1976). Formation and reaction of sulfenic acids in proteins. Accounts Chem. Res. 9, 293-299.
    • (1976) Accounts Chem. Res. , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 30
    • 0029053597 scopus 로고
    • Crystallographic analysis of NADH peroxidase Cys42Ala and Cys42Ser mutants: Active site structures, mechanistic implications, and an unusual environment of Arg303
    • Mande, S.S., Parsonage, D., Claiborne, A. & Hol, W.G.J. (1995). Crystallographic analysis of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg303. Biochemistry 34, 6985-6992.
    • (1995) Biochemistry , vol.34 , pp. 6985-6992
    • Mande, S.S.1    Parsonage, D.2    Claiborne, A.3    Hol, W.G.J.4
  • 31
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells, J.A. (1996). Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci. USA 93, 1-6.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 33
    • 13344270889 scopus 로고    scopus 로고
    • Structure based design of lipophillic quinazoline inhibitors of thymidylate synthase
    • Jones, T.R. et al., & Morse, C.A (1996). Structure based design of lipophillic quinazoline inhibitors of thymidylate synthase. J. Med. Chem. 39 904-917.
    • (1996) J. Med. Chem. , vol.39 , pp. 904-917
    • Jones, T.R.1    Morse, C.A.2
  • 34
    • 0029836936 scopus 로고    scopus 로고
    • Species-specific inhibition of homologous enzymes by modification of nonconserved amino acid residues. The cysteine residues of the triosephosphate isomerase
    • Garza-Ramos, G., Perez-Monfort, R., Rojo-Dominguewz, A., de Gomez-Puyou, M.T. (1996). Species-specific inhibition of homologous enzymes by modification of nonconserved amino acid residues. The cysteine residues of the triosephosphate isomerase. Eur. J. Biochem. 241, 144-120.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 144-1120
    • Garza-Ramos, G.1    Perez-Monfort, R.2    Rojo-Dominguewz, A.3    De Gomez-Puyou, M.T.4
  • 35
    • 0026546576 scopus 로고
    • Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: Effects of active site modification and deamidation
    • Sun, A.Q., Yuksel, K.U. & Gracy, R.W. (1992). Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation. Arch. Biochem. Biophys. 293, 382-390.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 382-390
    • Sun, A.Q.1    Yuksel, K.U.2    Gracy, R.W.3
  • 36
    • 0029070914 scopus 로고
    • The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum-infected erythrocyte
    • Su, X., et al., & Wellems, T.E. (1995). The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum-infected erythrocyte. Cell 82, 89-100.
    • (1995) Cell , vol.82 , pp. 89-100
    • Su, X.1    Wellems, T.E.2
  • 37
    • 0023942925 scopus 로고
    • Aldolase activity of a Plasmodium falciparum protein with protective properties
    • Certa, U., et al., & Perrin, L.R. (1988). Aldolase activity of a Plasmodium falciparum protein with protective properties. Science 240, 1036-1040.
    • (1988) Science , vol.240 , pp. 1036-1040
    • Certa, U.1    Perrin, L.R.2
  • 38
    • 0028944886 scopus 로고
    • Erythrocyte lipids in triosephosphate isomerase deficiency
    • Hollan, S., et al., & Farkas, T. (1995). Erythrocyte lipids in triosephosphate isomerase deficiency. Proc. Natl. Acad. Sci. USA 92, 268-271.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 268-271
    • Hollan, S.1    Farkas, T.2
  • 39
    • 0014829383 scopus 로고
    • Genetic mapping of a locus of triosephosphate isomerase on the locus of E. coli K12
    • Anderson, A. & Cooper, R.A. (1970). Genetic mapping of a locus of triosephosphate isomerase on the locus of E. coli K12. J. Gen. Microbiol. 62, 329-334.
    • (1970) J. Gen. Microbiol. , vol.62 , pp. 329-334
    • Anderson, A.1    Cooper, R.A.2
  • 41
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 study weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 43
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Berstein, F.C., et al., & Tasumi, M. (1977). The protein data bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Berstein, F.C.1    Tasumi, M.2
  • 45
    • 84889120137 scopus 로고
    • Improved methods for building models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowman, S.W. & Kjeldgaard, M. (1991). Improved methods for building models in electron-density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowman, S.W.3    Kjeldgaard, M.4
  • 46
    • 0026460334 scopus 로고
    • Molecular analysis of Plasmodium falciparum hexokinase
    • Olafsson, P., Matile, H. & Certa, U. (1992). Molecular analysis of Plasmodium falciparum hexokinase. Mol. Biochem. Parasitol. 56, 89-101.
    • (1992) Mol. Biochem. Parasitol. , vol.56 , pp. 89-101
    • Olafsson, P.1    Matile, H.2    Certa, U.3
  • 48
    • 0025832831 scopus 로고
    • Glycolytic pathway of the human malaria parasite Plasmodium falciparum: Primary sequence analysis of the gene encoding 3-phosphoglycerate kinase and chromosomal mapping studies
    • Hicks, K.E., Read, M., Holloway, S.P., Sims, P.F. & Hydwe, J.E. (1991). Glycolytic pathway of the human malaria parasite Plasmodium falciparum: primary sequence analysis of the gene encoding 3-phosphoglycerate kinase and chromosomal mapping studies. Gene 100, 123-129.
    • (1991) Gene , vol.100 , pp. 123-129
    • Hicks, K.E.1    Read, M.2    Holloway, S.P.3    Sims, P.F.4    Hydwe, J.E.5
  • 49
    • 0028280998 scopus 로고
    • Molecular characterization of the enolase gene from malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage
    • Read, M., Hicks, K.E., Sims, P.F. & Hyde, J.E. (1994). Molecular characterization of the enolase gene from malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage. Eur. J. Biochem. 220, 513-520.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 513-520
    • Read, M.1    Hicks, K.E.2    Sims, P.F.3    Hyde, J.E.4
  • 50
    • 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. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 51
    • 0003699451 scopus 로고
    • Biosym Technologies, San Diego, CA, USA
    • INSIGHTII (1993). Insight II user guide. Biosym Technologies, San Diego, CA, USA.
    • (1993) Insight II User Guide
  • 52
    • 0000732609 scopus 로고
    • GRASP: A graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: a graphical representation and analysis of surface properties. Biophys. J. 64, 166.
    • (1993) Biophys. J. , vol.64 , pp. 166
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


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