메뉴 건너뛰기




Volumn 12, Issue 3, 2003, Pages 501-509

Probing the structure of falcipain-3, a cysteine protease from Plasmodium falciparum: Comparative protein modeling and docking studies

Author keywords

Docking; Falcipain; Homology modeling; Plasmoditim falciparum

Indexed keywords

CYSTEINE PROTEINASE; FALCIPAIN 2; FALCIPAIN 3; UNCLASSIFIED DRUG;

EID: 0037370645     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0228103     Document Type: Article
Times cited : (62)

References (42)
  • 1
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch, A. and Apweiler, R. 2000. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acid Res. 28: 45-48.
    • (2000) Nucleic Acid Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 2
    • 0034972445 scopus 로고    scopus 로고
    • The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden
    • Breman, J.G. 2001. The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden. Am. J. Trop. Med. Hyg. 64: 1-11.
    • (2001) Am. J. Trop. Med. Hyg. , vol.64 , pp. 1-11
    • Breman, J.G.1
  • 3
    • 0034662749 scopus 로고    scopus 로고
    • A target within the target: Probing cruzain's P1′ site to define structural determinants for the Chagas' disease protease
    • Brinen, L.S., Hansell, E., Cheng, J., Roush, W.R., McKerrow, J.H., and Fletterick, R.J. 2000. A target within the target: Probing cruzain's P1′ site to define structural determinants for the Chagas' disease protease. Structure 8: 831-840.
    • (2000) Structure , vol.8 , pp. 831-840
    • Brinen, L.S.1    Hansell, E.2    Cheng, J.3    Roush, W.R.4    McKerrow, J.H.5    Fletterick, R.J.6
  • 4
    • 0031002808 scopus 로고    scopus 로고
    • Time to put malaria control on the global agenda
    • Butler, D., Maurice, J., and O'Brien, C. 1997. Time to put malaria control on the global agenda. Nature 386: 535-536.
    • (1997) Nature , vol.386 , pp. 535-536
    • Butler, D.1    Maurice, J.2    O'Brien, C.3
  • 5
    • 0033533253 scopus 로고    scopus 로고
    • The 2.1 Å structure of a cysteine protease with proline specificity from ginger rhizome. Zingiber officinale
    • Choi, H.K., Laursen, R.A., and Allen, K.N. 1999. The 2.1 Å structure of a cysteine protease with proline specificity from ginger rhizome. Zingiber officinale. Biochemistry 38: 11624-11633.
    • (1999) Biochemistry , vol.38 , pp. 11624-11633
    • Choi, H.K.1    Laursen, R.A.2    Allen, K.N.3
  • 7
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson, K.K., Duffin, K.L., and Goldberg, D.E. 1999. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J. Biol. Chem. 274: 32411-32417.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 8
    • 0013418179 scopus 로고    scopus 로고
    • Integrated homology modeling and X-ray study of herpes simplex virus I thymidine kinase
    • (ed. P.W. Codding), Kluwer Academic Publishers, Norwell, MA, USA
    • Folkers, G. 1998. Integrated homology modeling and X-ray study of herpes simplex virus I thymidine kinase. In Structure-based rug design experimental and computational approaches (ed. P.W. Codding), pp. 271-283. Kluwer Academic Publishers, Norwell, MA, USA.
    • (1998) Structure-based Rug Design Experimental and Computational Approaches , pp. 271-283
    • Folkers, G.1
  • 10
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • Gillmor, S.A., Craik, C.S., and Fletterick, R.J. 1997. Structural determinants of specificity in the cysteine protease cruzain. Protein Sci. 6: 1603-1611.
    • (1997) Protein Sci. , vol.6 , pp. 1603-1611
    • Gillmor, S.A.1    Craik, C.S.2    Fletterick, R.J.3
  • 12
    • 0026726481 scopus 로고
    • Topology finger print approach to the inverse protein folding problem
    • Godzik, A., Kolinski, A., and Skolnick, J. 1992. Topology finger print approach to the inverse protein folding problem. J. Mol. Biol. 227: 227-238.
    • (1992) J. Mol. Biol. , vol.227 , pp. 227-238
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 13
    • 0037134034 scopus 로고    scopus 로고
    • Parasitology: When the host is smarter than the parasite
    • Goldberg, D.E. 2002. Parasitology: When the host is smarter than the parasite. Science 296: 482-483.
    • (2002) Science , vol.296 , pp. 482-483
    • Goldberg, D.E.1
  • 14
    • 0000396658 scopus 로고
    • A fast algorithm for particle simulations
    • Greengard, L. and Rokhlin, V.I. 1987. A fast algorithm for particle simulations. J. Comp. Phys. 73: 325-348.
    • (1987) J. Comp. Phys. , vol.73 , pp. 325-348
    • Greengard, L.1    Rokhlin, V.I.2
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D.T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292: 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 16
    • 0035997361 scopus 로고    scopus 로고
    • Biological roles of proteases in parasitic protozoa
    • Klemba, M. and Goldberg, D.E. 2002. Biological roles of proteases in parasitic protozoa. Annu. Rev. Biochem. 71: 275-305.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 275-305
    • Klemba, M.1    Goldberg, D.E.2
  • 17
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung, D., Abbenante, G., and Fairlie, D.P. 2000. Protease inhibitors: Current status and future prospects. J. Med. Chem. 43: 305-341.
    • (2000) J. Med. Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 18
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., Bowie, J.U., and Eisenberg, D. 1992. Assessment of protein models with three-dimensional profiles. Nature 356: 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 21
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K., and Jones, D.T. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 22
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. and Wunsch, C. 1970. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48: 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.1    Wunsch, C.2
  • 23
    • 0033004991 scopus 로고    scopus 로고
    • An overview of chemotherapeutic targets for antimalarial drug discovery
    • Olliaro, P.L. and Yuthavong, Y. 1999. An overview of chemotherapeutic targets for antimalarial drug discovery. Pharm. Ther. 81: 91-110.
    • (1999) Pharm. Ther. , vol.81 , pp. 91-110
    • Olliaro, P.L.1    Yuthavong, Y.2
  • 24
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • Olson, J.E., Lee, G.K., Semenov, A., and Rosenthal, P.J. 1999. Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorg. Med. Chem. 7: 633-638.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 26
    • 0031852685 scopus 로고    scopus 로고
    • Proteases of malaria parasites: New targets for chemotherapy
    • Rosenthal, P. 1998. Proteases of malaria parasites: New targets for chemotherapy. Emerg. Infect. Dis. 4: 49-56.
    • (1998) Emerg. Infect. Dis. , vol.4 , pp. 49-56
    • Rosenthal, P.1
  • 27
    • 0036183460 scopus 로고    scopus 로고
    • Hydrolysis of erythrocyte proteins by proteases of malaria parasites
    • Rosenthal, P.J. 2002. Hydrolysis of erythrocyte proteins by proteases of malaria parasites. Curr. Opin. Hematol. 9: 140-145.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 140-145
    • Rosenthal, P.J.1
  • 28
    • 0030596209 scopus 로고    scopus 로고
    • Hemoglobin catabolism and iron utilization by malaria parasites
    • Rosenthal, P.J. and Meshnick, S.R. 1996. Hemoglobin catabolism and iron utilization by malaria parasites. Mol. Biochem. Parasitol. 83: 131-139.
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 131-139
    • Rosenthal, P.J.1    Meshnick, S.R.2
  • 29
    • 0025719869 scopus 로고
    • Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase
    • Rosenthal, P.J., Wollish, W.S., Palmer, J.T., and Rasnick, D. 1991. Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase. J. Clin. Invest. 88: 1467-1472.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1467-1472
    • Rosenthal, P.J.1    Wollish, W.S.2    Palmer, J.T.3    Rasnick, D.4
  • 30
    • 0027512171 scopus 로고
    • Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria
    • Rosenthal, P.J., Lee, G.K., and Smith, R.E. 1993. Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria. J. Clin. Invest. 91: 1052-1056.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1052-1056
    • Rosenthal, P.J.1    Lee, G.K.2    Smith, R.E.3
  • 32
    • 0036244780 scopus 로고    scopus 로고
    • Homology modeling of falcipain-2: Validation, de novo ligand design and synthesis of novel inhibitors
    • Sabnis, Y., Rosenthal, P.J., Desai, P., and Avery, M.A. 2002. Homology modeling of falcipain-2: Validation, de novo ligand design and synthesis of novel inhibitors. J. Biomol. Struct. Dyn. 19: 765-774.
    • (2002) J. Biomol. Struct. Dyn. , vol.19 , pp. 765-774
    • Sabnis, Y.1    Rosenthal, P.J.2    Desai, P.3    Avery, M.A.4
  • 33
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid, M. and McKerrow, J.H. 2002. Cysteine proteases of parasitic organisms. Mol. Biochem. Parasitol. 120: 1-21.
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 34
    • 0029057887 scopus 로고
    • Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase
    • Salas, F., Fichmann, J., Lee, G.K., Scott, M.D., and Rosenthal, P.J. 1995. Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase. Infect. Immun. 63: 2120-2125.
    • (1995) Infect. Immun. , vol.63 , pp. 2120-2125
    • Salas, F.1    Fichmann, J.2    Lee, G.K.3    Scott, M.D.4    Rosenthal, P.J.5
  • 36
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai, B.R., Sijwali, P.S., Singh, A., and Rosenthal, P.J. 2000. Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J. Biol. Chem. 275: 29000-29010.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 37
    • 0022842039 scopus 로고
    • Predicting antibody hypervariable loop conformations II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations
    • Shenkin, P.S., Yarmush, D.L., Fine, R.M., Wang, H., and Levinthal, C. 1986. Predicting antibody hypervariable loop conformations II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations. Proteins Struct. Funct. Genet. 1: 342-362.
    • (1986) Proteins Struct. Funct. Genet. , vol.1 , pp. 342-362
    • Shenkin, P.S.1    Yarmush, D.L.2    Fine, R.M.3    Wang, H.4    Levinthal, C.5
  • 38
    • 0023478807 scopus 로고
    • Predicting antibody hypervariable loop conformation. I. Ensembles of random conformations for ringlike structures
    • -. 1987. Predicting antibody hypervariable loop conformation. I. Ensembles of random conformations for ringlike structures. Biopolymers 26: 2053-2085.
    • (1987) Biopolymers , vol.26 , pp. 2053-2085
  • 39
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum hemoglobinase falcipain-3
    • Sijwali, P.S., Shenai, B.R., Gut, J., Singh, A., and Rosenthal, P.J. 2001. Expression and characterization of the Plasmodium falciparum hemoglobinase falcipain-3. Biochem. J. 360: 481-489.
    • (2001) Biochem. J. , vol.360 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.4    Rosenthal, P.J.5
  • 40
    • 0027804108 scopus 로고
    • An effective solvation term based on atomic occupancies for use in protein simulations
    • Stouten, P.F.W., Froemmel, C., Nakamura, H., and Sander, C. 1993. An effective solvation term based on atomic occupancies for use in protein simulations. Mol. Simul. 10: 97-120.
    • (1993) Mol. Simul. , vol.10 , pp. 97-120
    • Stouten, P.F.W.1    Froemmel, C.2    Nakamura, H.3    Sander, C.4
  • 41
    • 22944467757 scopus 로고
    • Computer "experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules
    • Verlet, L. 1967. Computer "experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules. Phys. Rev. 159: 98-103.
    • (1967) Phys. Rev. , vol.159 , pp. 98-103
    • Verlet, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.