메뉴 건너뛰기




Volumn 353, Issue 3, 2005, Pages 584-599

Structures for the potential drug target purine nucleoside phosphorylase from Schistosoma mansoni causal agent of schistosomiasis

Author keywords

Crystal structure; Non detergent sulfobetaine 195; PNP complexes; Purine nucleoside phosphorylase; Schistosoma mansoni

Indexed keywords

ACETIC ACID; BETAINE DERIVATIVE; HYPOXANTHINE; NUCLEOSIDE; PHOSPHATE; PURINE NUCLEOSIDE PHOSPHORYLASE; RIBOSE;

EID: 26444499643     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.045     Document Type: Article
Times cited : (35)

References (46)
  • 1
    • 0036103409 scopus 로고    scopus 로고
    • Recent investigations of artemether, a novel agent for the prevention of schistosomiasis japonica, mansoni and hematobia
    • X. Shuhua, M. Tanner, E.K. N'Goran, J. Utzinger, J. Chollet, and R. Bergquist Recent investigations of artemether, a novel agent for the prevention of schistosomiasis japonica, mansoni and hematobia Acta Trop. 82 2002 175 181
    • (2002) Acta Trop. , vol.82 , pp. 175-181
    • Shuhua, X.1    Tanner, M.2    N'Goran, E.K.3    Utzinger, J.4    Chollet, J.5    Bergquist, R.6
  • 5
    • 16544371718 scopus 로고    scopus 로고
    • Determination of ED50 values for praziquantel in praziquantel-resistant and -susceptible Schistosoma mansoni isolates
    • D. Cioli, S.S. Botros, K. Wheatcroft-Francklow, A. Mbaye, V. Southgate, and L.A. Tchuente Determination of ED50 values for praziquantel in praziquantel-resistant and -susceptible Schistosoma mansoni isolates Int. J. Parasitol. 34 2004 979 987
    • (2004) Int. J. Parasitol. , vol.34 , pp. 979-987
    • Cioli, D.1    Botros, S.S.2    Wheatcroft-Francklow, K.3    Mbaye, A.4    Southgate, V.5    Tchuente, L.A.6
  • 8
    • 0015924014 scopus 로고
    • Pathways of nucleotide metabolism in Schistosoma mansoni. II. Disposition of adenosine by whole worms
    • A.W. Senft, D.G. Senft, and R.P. Miech Pathways of nucleotide metabolism in Schistosoma mansoni. II. Disposition of adenosine by whole worms Biochem. Phamarcol. 22 1973 437 447
    • (1973) Biochem. Phamarcol. , vol.22 , pp. 437-447
    • Senft, A.W.1    Senft, D.G.2    Miech, R.P.3
  • 9
    • 0015924018 scopus 로고
    • Pathways of nucleotide metabolism in Schistosoma mansoni. III. Identification of enzymes in cell-free extracts
    • A.W. Senft, G.W. Crabtree, K.C. Agarwal, E.M. Scholar, R.P. Agarwal, and R.E. Parks Pathways of nucleotide metabolism in Schistosoma mansoni. III. Identification of enzymes in cell-free extracts Biochem. Pharmacol. 22 1973 449 458
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 449-458
    • Senft, A.W.1    Crabtree, G.W.2    Agarwal, K.C.3    Scholar, E.M.4    Agarwal, R.P.5    Parks, R.E.6
  • 10
    • 0017725417 scopus 로고
    • Pathways of nucleotide metabolism in Schistosoma mansoni. VII. Inhibition of adenine and guanine nucleotide synthesis by purine analogs in intact worms
    • A.W. Senft, and G.W. Crabtree Pathways of nucleotide metabolism in Schistosoma mansoni. VII. Inhibition of adenine and guanine nucleotide synthesis by purine analogs in intact worms Biochem. Pharmacol. 26 1977 1847 1855
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 1847-1855
    • Senft, A.W.1    Crabtree, G.W.2
  • 12
    • 0020576382 scopus 로고
    • Purine metabolism in the schistosomoses: Potential targets for chemotherapy
    • A.W. Senft, and G.W. Crabtree Purine metabolism in the schistosomoses: potential targets for chemotherapy Pharmacol. Ther. 20 1983 341 356
    • (1983) Pharmacol. Ther. , vol.20 , pp. 341-356
    • Senft, A.W.1    Crabtree, G.W.2
  • 13
    • 84919573117 scopus 로고
    • Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity
    • E.R. Giblett, A.J. Ammann, D.W. Wara, R. Sandman, and L.K. Diamond Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity Lancet 1 1975 1010 1013
    • (1975) Lancet , vol.1 , pp. 1010-1013
    • Giblett, E.R.1    Ammann, A.J.2    Wara, D.W.3    Sandman, R.4    Diamond, L.K.5
  • 14
    • 0001157528 scopus 로고
    • Purine nucleoside phosphorylase: A target for chemotherapy
    • R.I. Glazer CRC Press Boca Raton
    • J.D. Stoeckler Purine nucleoside phosphorylase: a target for chemotherapy R.I. Glazer Developments in Cancer Chemotherapy 1984 CRC Press Boca Raton 35 60
    • (1984) Developments in Cancer Chemotherapy , pp. 35-60
    • Stoeckler, J.D.1
  • 15
    • 0018598669 scopus 로고
    • Allopurinol ribonucleoside as an antileishmanial agent. Biological effects, metabolism, and enzymatic phosphorylation
    • D.J. Nelson, S.W. LaFon, J.V. Tuttle, W.H. Miller, R.L. Miller, and T.A. Krenisky Allopurinol ribonucleoside as an antileishmanial agent. Biological effects, metabolism, and enzymatic phosphorylation J. Biol. Chem. 254 1979 11544 11549
    • (1979) J. Biol. Chem. , vol.254 , pp. 11544-11549
    • Nelson, D.J.1    Lafon, S.W.2    Tuttle, J.V.3    Miller, W.H.4    Miller, R.L.5    Krenisky, T.A.6
  • 16
    • 0034452004 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylases: Properities, functions, and clinical aspects
    • A. Bzowska, E. Kulikowska, and D. Shugar Purine nucleoside phosphorylases: properities, functions, and clinical aspects Pharm. Ther. 88 2000 349 425
    • (2000) Pharm. Ther. , vol.88 , pp. 349-425
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 17
    • 0036479331 scopus 로고    scopus 로고
    • Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum
    • G.A. Kicska, P.C. Tyler, G.B. Evans, R.H. Furneaux, V.L. Schramm, and K. Kim Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum J. Mol. Biol. 277 2002 3226 3231
    • (2002) J. Mol. Biol. , vol.277 , pp. 3226-3231
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Schramm, V.L.5    Kim, K.6
  • 19
    • 0031575420 scopus 로고    scopus 로고
    • Crystal structure of calf spleen purine nucleoside phosphorylase in a complex withypoxanthine at 2.15 Å resolution
    • G. Koellner, M. Luic, D. Shugar, W. Saenger, and A. Bzowska Crystal structure of calf spleen purine nucleoside phosphorylase in a complex withypoxanthine at 2.15 Å resolution J. Mol. Biol 265 1997 202 216
    • (1997) J. Mol. Biol , vol.265 , pp. 202-216
    • Koellner, G.1    Luic, M.2    Shugar, D.3    Saenger, W.4    Bzowska, A.5
  • 20
    • 0025021597 scopus 로고
    • Three dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 Å resolution
    • S.E. Ealick, S.A. Rule, D.C. Carter, T.J. Greenhough, Y.S. Babu, and W.J. Cook Three dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 Å resolution J. Biol. Chem. 265 1990 1812 1820
    • (1990) J. Biol. Chem. , vol.265 , pp. 1812-1820
    • Ealick, S.E.1    Rule, S.A.2    Carter, D.C.3    Greenhough, T.J.4    Babu, Y.S.5    Cook, W.J.6
  • 21
    • 0030887917 scopus 로고    scopus 로고
    • Refined structure of purine nucleoside phosphorylase at 2.75 Å resolution
    • S.V.L. Narayana, C.E. Bugg, and S.E. Ealick Refined structure of purine nucleoside phosphorylase at 2.75 Å resolution Acta Crystallog. sect. D 53 1997 131 142
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 131-142
    • Narayana, S.V.L.1    Bugg, C.E.2    Ealick, S.E.3
  • 22
    • 0033579544 scopus 로고    scopus 로고
    • Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs
    • J. Tebbe, A. Bzowska, B. Wielgus-Kutrowska, W. Schroder, Z. Kazimierczuk, and D. Shugar Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs J. Mol. Biol. 294 1999 1239 1255
    • (1999) J. Mol. Biol. , vol.294 , pp. 1239-1255
    • Tebbe, J.1    Bzowska, A.2    Wielgus-Kutrowska, B.3    Schroder, W.4    Kazimierczuk, Z.5    Shugar, D.6
  • 23
    • 0035902502 scopus 로고    scopus 로고
    • Structure of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucilin-H and its pieces
    • W. Shi, L.A. Basso, D.S. Santos, P.C. Tyler, R.H. Furneaux, and J.S. Blanchard Structure of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucilin-H and its pieces Biochemistry 40 2001 8204 8215
    • (2001) Biochemistry , vol.40 , pp. 8204-8215
    • Shi, W.1    Basso, L.A.2    Santos, D.S.3    Tyler, P.C.4    Furneaux, R.H.5    Blanchard, J.S.6
  • 25
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J. 4 1986 823 826
    • (1986) EMBO J. , vol.4 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 26
    • 0016442129 scopus 로고
    • Purine nucleoside phosphorylase microheterogeneity and comparison of kinetic behavior of the enzyme from several tissues and species
    • K.C. Agarwal, R.P. Agarwal, J.D. Stoeckler, and R.E. Parks; Purine nucleoside phosphorylase microheterogeneity and comparison of kinetic behavior of the enzyme from several tissues and species Biochemistry 14 1975 79 84
    • (1975) Biochemistry , vol.14 , pp. 79-84
    • Agarwal, K.C.1    Agarwal, R.P.2    Stoeckler, J.D.3    Parks4    parks, R.E.5
  • 28
    • 0032546620 scopus 로고    scopus 로고
    • Calf speen purine nucleoside phosphorylase complexed with substrates and substrates analogues
    • C. Mao, W.J. Cook, M. Zhou, A.A. Federov, S.C. Almo, and S.E. Ealick Calf speen purine nucleoside phosphorylase complexed with substrates and substrates analogues Biochemistry 37 1998 7135 7146
    • (1998) Biochemistry , vol.37 , pp. 7135-7146
    • Mao, C.1    Cook, W.J.2    Zhou, M.3    Federov, A.A.4    Almo, S.C.5    Ealick, S.E.6
  • 29
    • 4444273108 scopus 로고    scopus 로고
    • Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: Important implications for the mechanism of catalysis
    • A. Bzowska, G. Koellner, B. Wielgus-Kutrowska, A. Stroh, G. Raszewski, and A. Holy Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis J. Mol. Biol. 342 2004 1015 1032
    • (2004) J. Mol. Biol. , vol.342 , pp. 1015-1032
    • Bzowska, A.1    Koellner, G.2    Wielgus-Kutrowska, B.3    Stroh, A.4    Raszewski, G.5    Holy, A.6
  • 30
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • G. Jones, P. Willett, R.C. Glen, A.R. Leach, and R. Taylor Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 267 1997 727 748
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 31
    • 0038044740 scopus 로고    scopus 로고
    • Cloning, expression and preliminary crystallographic studies of the potential drug target purine nucleoside phosphorylase from Schistosoma mansoni
    • H.M. Pereira, A. Cleasby, S.D.J. Pena, G.R. Franco, and R.C. Garratt Cloning, expression and preliminary crystallographic studies of the potential drug target purine nucleoside phosphorylase from Schistosoma mansoni Acta Crystallog. sect. D 59 2003 1096 1099
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 1096-1099
    • Pereira, H.M.1    Cleasby, A.2    Pena, S.D.J.3    Franco, G.R.4    Garratt, R.C.5
  • 33
    • 0026705348 scopus 로고
    • Purine nucleoside phosphorylase. Kinetic mechanism of the enzyme from calf spleen
    • D.J. Porter Purine nucleoside phosphorylase. Kinetic mechanism of the enzyme from calf spleen J. Biol. Chem. 267 1992 7342 7351
    • (1992) J. Biol. Chem. , vol.267 , pp. 7342-7351
    • Porter, D.J.1
  • 34
    • 0036680063 scopus 로고    scopus 로고
    • Protein flexibility and drug design: How to hit a moving target
    • H.A. Carlson Protein flexibility and drug design: how to hit a moving target Curr. Opin. Chem. Biol. 4 2002 447 452
    • (2002) Curr. Opin. Chem. Biol. , vol.4 , pp. 447-452
    • Carlson, H.A.1
  • 35
    • 0027458426 scopus 로고
    • Structure-based design of inhibitors of purine nucleoside phosphorylase. 1. 9-(Arylmethyl) derivatives of 9-deazaguanine
    • J.A. Montgomery, S. Niwas, J.D. Rose, J. Secrist 3rd., Y.S. Babu, and C.E. Bugg Structure-based design of inhibitors of purine nucleoside phosphorylase. 1. 9-(Arylmethyl) derivatives of 9-deazaguanine J. Med. Chem. 36 1993 55 69
    • (1993) J. Med. Chem. , vol.36 , pp. 55-69
    • Montgomery, J.A.1    Niwas, S.2    Rose, J.D.3    Secrist III, J.4    Babu, Y.S.5    Bugg, C.E.6
  • 36
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • A.G.W. Leslie Integration of macromolecular diffraction data Acta Crystallog. sect. D 55 1999 1696 1702
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 38
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • A. Vagin, and A. Teplyakov An approach to multi-copy search in molecular replacement Acta Crystallog. sect. D 56 2000 1622 1624
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 40
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1
  • 41
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallog. sect. D 57 2001 122 133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 42
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R.M. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.M.2    Lamzin, V.S.3
  • 43
    • 0035022345 scopus 로고    scopus 로고
    • X-LIGAND: An application for the automated addition of flexible ligands into electron density
    • T.J Oldfield X-LIGAND: an application for the automated addition of flexible ligands into electron density Acta Crystallog. sect. D 57 2001 696 705
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 696-705
    • Oldfield, T.J.1
  • 45
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.