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Volumn 48, Issue 4, 2001, Pages 903-916

Computer modeling studies of the structural role of NADPH binding to active site mutants of human dihydrofolate reductase in complex with piritrexim

Author keywords

Chemotherapy; Computer modeling; Dihydrofolate reductase; Enzyme structure; ESFF forcefield; NADPH; Piritrexim

Indexed keywords

ANTINEOPLASTIC AGENT; DIHYDROFOLATE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PIRITREXIM; PYRIMIDINE DERIVATIVE;

EID: 0035756319     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2001_3856     Document Type: Article
Times cited : (3)

References (36)
  • 2
    • 0001845556 scopus 로고    scopus 로고
    • New antifolates: Pharmacology and clinical applications
    • Takimoto, C.H. (1996) New antifolates: Pharmacology and clinical applications. Oncologist 1, 68-81.
    • (1996) Oncologist , vol.1 , pp. 68-81
    • Takimoto, C.H.1
  • 3
    • 0031581179 scopus 로고    scopus 로고
    • Comparison of the protection of cells from antifolates by transduced human dihydrofolate reductase mutants
    • Patel, M., Sleep, S.E., Lewis, W.S., Spencer, H.T., Mareya, S.M., Sorrentino, B.P. & Blakley, R.L. (1997) Comparison of the protection of cells from antifolates by transduced human dihydrofolate reductase mutants. Hum. Gene Ther. 8, 2069-2077.
    • (1997) Hum. Gene Ther. , vol.8 , pp. 2069-2077
    • Patel, M.1    Sleep, S.E.2    Lewis, W.S.3    Spencer, H.T.4    Mareya, S.M.5    Sorrentino, B.P.6    Blakley, R.L.7
  • 4
    • 0028241517 scopus 로고
    • Methotrexate-resistant variants of human dihydrofolate reductase. Effects of Phe31 substitutions
    • Chunduru, S. K., Cody, V., Luft, J.R., Pangborn, W., Appleman, J.R. & Blakley, R.L. (1994) Methotrexate-resistant variants of human dihydrofolate reductase. Effects of Phe31 substitutions. J. Biol. Chem. 269, 9547-9555.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9547-9555
    • Chunduru, S.K.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4    Appleman, J.R.5    Blakley, R.L.6
  • 5
    • 0028920025 scopus 로고
    • Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers
    • Lewis, W.S., Cody, V., Galitsky, N., Luft, J.R., Pangborn, W., Chunduru, S.K., Spencer, H.T., Appleman, J.R. & Blakley, R.L. (1995) Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers. J. Biol Chem. 270, 5057-5064.
    • (1995) J. Biol Chem. , vol.270 , pp. 5057-5064
    • Lewis, W.S.1    Cody, V.2    Galitsky, N.3    Luft, J.R.4    Pangborn, W.5    Chunduru, S.K.6    Spencer, H.T.7    Appleman, J.R.8    Blakley, R.L.9
  • 6
    • 0018874182 scopus 로고
    • Synthesis and antitumor activity of 2,4-diamino-6-(2,5-dimethoxybenzyl)-5-me-thylpyrido[2,3-d]pyrimidine
    • Grivsky, E.M., Lee, S., Sigel, C.W. & Nichol, C.A. (1980) Synthesis and antitumor activity of 2,4-diamino-6-(2,5-dimethoxybenzyl)-5-me-thylpyrido[2,3-d]pyrimidine. J. Med. Chem. 23, 327-329.
    • (1980) J. Med. Chem. , vol.23 , pp. 327-329
    • Grivsky, E.M.1    Lee, S.2    Sigel, C.W.3    Nichol, C.A.4
  • 7
    • 0030927578 scopus 로고    scopus 로고
    • Phase II trial of oral piritrexim in advanced, previously treated transitional cell cancer of bladder
    • Khorsand, M., Lange, J., Feun, L., Clendeninn, N.J., Collier, M. & Wilding, G. (1997) Phase II trial of oral piritrexim in advanced, previously treated transitional cell cancer of bladder. Invest. New Drugs 15, 157-163.
    • (1997) Invest. New Drugs , vol.15 , pp. 157-163
    • Khorsand, M.1    Lange, J.2    Feun, L.3    Clendeninn, N.J.4    Collier, M.5    Wilding, G.6
  • 8
    • 0035913056 scopus 로고    scopus 로고
    • Design, synthesis, computational prediction, and biological evaluation of ester soft drugs as inhibitors of dihydrofolate reductase from Pneumocystis carinii
    • Graffner-Nordberg, M., Kolmodin, K., Aqvist, J., Queener, S.F. & Hallberg, A. (2001) Design, synthesis, computational prediction, and biological evaluation of ester soft drugs as inhibitors of dihydrofolate reductase from Pneumocystis carinii. J. Med. Chem. 44, 2391-2402.
    • (2001) J. Med. Chem. , vol.44 , pp. 2391-2402
    • Graffner-Nordberg, M.1    Kolmodin, K.2    Aqvist, J.3    Queener, S.F.4    Hallberg, A.5
  • 9
    • 0034007479 scopus 로고    scopus 로고
    • Dihydrofolate reductase from Kaposi's sarcoma-associated herpesvirus
    • Cinquina, C.C., Grogan, E., Sun, R., Lin, S.F., Beardsley, G.P. & Miller, G. (2000) Dihydrofolate reductase from Kaposi's sarcoma-associated herpesvirus. Virology 268, 201-217.
    • (2000) Virology , vol.268 , pp. 201-217
    • Cinquina, C.C.1    Grogan, E.2    Sun, R.3    Lin, S.F.4    Beardsley, G.P.5    Miller, G.6
  • 11
    • 0039637846 scopus 로고    scopus 로고
    • Computer modeling of human dihydrofolate reductase ternary complex with NADPH and piritreim (PTX) inhibitor
    • Nowak, W., Wojtczak, A. & Cody, V. (1999) Computer modeling of human dihydrofolate reductase ternary complex with NADPH and piritreim (PTX) inhibitor. Internet J. Chem. 12, www.ijc.com/articles/1999v2/50/.
    • (1999) Internet J. Chem. , vol.12
    • Nowak, W.1    Wojtczak, A.2    Cody, V.3
  • 12
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M.R. & Kraut, J. (1997) Loop and subdomain movements in mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence. Biochemistry 36, 586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 13
    • 0031808658 scopus 로고    scopus 로고
    • Stretching exercises - Flexibility in dihydrofolate reductase catalysis
    • Miller, P.G. & Benkovic, S.J. (1998) Stretching exercises - flexibility in dihydrofolate reductase catalysis. Chem. Biol. 5, R105-R113.
    • (1998) Chem. Biol. , vol.5
    • Miller, P.G.1    Benkovic, S.J.2
  • 14
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of flexibility in the catalytic mechanism
    • Osborne, M.J., Schnell, J., Benkovic, S.J., Dyson, H.J. & Wright, P.E. (2001) Backbone dynamics in dihydrofolate reductase complexes: Role of flexibility in the catalytic mechanism. Biochemistry 40, 9846-9859.
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 15
    • 0030936561 scopus 로고    scopus 로고
    • NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase
    • Johnson, J.M., Meiering, E.M., Wright, J.E., Pardo, J., Rosowsky, A. & Wagner, G. (1997) NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase. Biochemistry 36, 4399-4411.
    • (1997) Biochemistry , vol.36 , pp. 4399-4411
    • Johnson, J.M.1    Meiering, E.M.2    Wright, J.E.3    Pardo, J.4    Rosowsky, A.5    Wagner, G.6
  • 16
    • 0030656217 scopus 로고    scopus 로고
    • Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523
    • Cody, V., Galitsky, N., Luft, J.R., Pangborn, W., Rosowsky, A. & Blakley, R.L. (1997) Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. Biochemistry 36, 13897-13903.
    • (1997) Biochemistry , vol.36 , pp. 13897-13903
    • Cody, V.1    Galitsky, N.2    Luft, J.R.3    Pangborn, W.4    Rosowsky, A.5    Blakley, R.L.6
  • 17
    • 0034710950 scopus 로고    scopus 로고
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble
    • Pan, H., Lee, J.C. & Hilser, V.J. (2000) Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. Proc. Natl. Acad. Sci. U.S.A. 97, 12020-12025.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12020-12025
    • Pan, H.1    Lee, J.C.2    Hilser, V.J.3
  • 18
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff, C. & Kraut, J. (1991) Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry 30, 2227-2239.
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 19
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo, O. & Argos, P. (1997) NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins 28, 10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 20
    • 0035974647 scopus 로고    scopus 로고
    • X-Ray crystal structures of Candida albicans dihydrofolate reductase: High resolution ternary complexes in which the dihydronicotinamide moiety of NADPH is displaced by an inhibitor
    • Whitlow, M., Howard, A.J., Stewart, D., Hardman, K.D, Chan, J.H., Baccanari, D.P., Tansik, R.L., Hong, J.S. & Kuyper, L.F. (2001) X-Ray crystal structures of Candida albicans dihydrofolate reductase: High resolution ternary complexes in which the dihydronicotinamide moiety of NADPH is displaced by an inhibitor. J. Med. Chem. 44, 2928-2932.
    • (2001) J. Med. Chem. , vol.44 , pp. 2928-2932
    • Whitlow, M.1    Howard, A.J.2    Stewart, D.3    Hardman, K.D.4    Chan, J.H.5    Baccanari, D.P.6    Tansik, R.L.7    Hong, J.S.8    Kuyper, L.F.9
  • 21
    • 0031557394 scopus 로고    scopus 로고
    • Domain motions in dihydrofolate reductase: A molecular dynamics study
    • Verma, C.S., Caves, L.D.S., Hubbard, R.E. & Roberts, G.C.K. (1997). Domain motions in dihydrofolate reductase: A molecular dynamics study. J. Mol. Biol. 266, 776-796.
    • (1997) J. Mol. Biol. , vol.266 , pp. 776-796
    • Verma, C.S.1    Caves, L.D.S.2    Hubbard, R.E.3    Roberts, G.C.K.4
  • 23
    • 0033927192 scopus 로고    scopus 로고
    • Interaction energy analyses of folate analog binding to human dihydrofolate reductase: Contribution of the antifolate substructural regions to complex stability
    • Pitts, C., Bowen, D. & Southerland, W.M. (2000) Interaction energy analyses of folate analog binding to human dihydrofolate reductase: Contribution of the antifolate substructural regions to complex stability. Drug Metabol. Drug Interact. 16, 99-121.
    • (2000) Drug Metabol. Drug Interact. , vol.16 , pp. 99-121
    • Pitts, C.1    Bowen, D.2    Southerland, W.M.3
  • 24
    • 84961978282 scopus 로고    scopus 로고
    • Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase
    • Cummins, P.L. & Gready, J.E. (2001) Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase. J. Am. Chem. Soc. 123, 3418-3428.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3418-3428
    • Cummins, P.L.1    Gready, J.E.2
  • 26
    • 0035107735 scopus 로고    scopus 로고
    • Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: Relative stabilities in experiment and simulations
    • Sham, Y.Y., Ma, B., Tsai, C.J. & Nussinov, R. (2001) Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: Relative stabilities in experiment and simulations. Protein Sci. 10, 135-348.
    • (2001) Protein Sci. , vol.10 , pp. 135-348
    • Sham, Y.Y.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 27
    • 0029782448 scopus 로고    scopus 로고
    • Molecular mechanics study of oligomeric models for poly(ferrocenylsilanes) using the Extensible Systematic Forcefield (ESFF)
    • Barlow, S., Rohl, A.L., Shi, S.G., Freeman, C.M. & O'Hare, D. (1996) Molecular mechanics study of oligomeric models for poly(ferrocenylsilanes) using the Extensible Systematic Forcefield (ESFF). J. Am. Chem. Soc. 118, 7578-7592.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7578-7592
    • Barlow, S.1    Rohl, A.L.2    Shi, S.G.3    Freeman, C.M.4    O'Hare, D.5
  • 28
    • 0003454656 scopus 로고    scopus 로고
    • Molecular Simulations Inc., San Diego
    • Forcefield-Based Simulations' (1997) Molecular Simulations Inc., San Diego.
    • (1997) Forcefield-Based Simulations
  • 29
    • 48749148224 scopus 로고
    • RATTLE: A velocity version of the SHAKE algorithm for molecular dynamics
    • Andersen, H.C. (1983) RATTLE: A velocity version of the SHAKE algorithm for molecular dynamics. J. Comp. Physics 52, 24-34.
    • (1983) J. Comp. Physics , vol.52 , pp. 24-34
    • Andersen, H.C.1
  • 30
    • 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. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0022546047 scopus 로고
    • Functional role of aspartic acid-27 in dihydrofolate aeductase revealed by mutagenesis
    • Howell, E.E., Villafranca, J.E., Warren, M.S., Oatley, S.J. & Kraut, J. (1986) Functional role of aspartic acid-27 in dihydrofolate aeductase revealed by mutagenesis. Science 231, 1123-1128.
    • (1986) Science , vol.231 , pp. 1123-1128
    • Howell, E.E.1    Villafranca, J.E.2    Warren, M.S.3    Oatley, S.J.4    Kraut, J.5
  • 34
    • 0034645774 scopus 로고    scopus 로고
    • Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs
    • Li, R., Sirawaraporn, R., Chitnumsub, P., Sirawaraporn, W., Wooden, J., Athappilly, F., Turley, S. & Hol, W.G. (2000) Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. J. Mol. Biol. 295, 307-323.
    • (2000) J. Mol. Biol. , vol.295 , pp. 307-323
    • Li, R.1    Sirawaraporn, R.2    Chitnumsub, P.3    Sirawaraporn, W.4    Wooden, J.5    Athappilly, F.6    Turley, S.7    Hol, W.G.8
  • 36
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993) SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1


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