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Volumn 6, Issue 11, 1998, Pages 1467-1479

The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation

Author keywords

Domain movement; Gliostatin; Platelet derived endothelial cell growth factor; Thymidine phosphorylase

Indexed keywords


EID: 0032533446     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00145-2     Document Type: Article
Times cited : (67)

References (39)
  • 1
    • 0030199507 scopus 로고    scopus 로고
    • Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2
    • Hamamoto, T., Noguchi, T. & Midorikawa, Y. (1996). Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2. Biosci. Biotech. Biochem. 60 (7), 1179-1180.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , Issue.7 , pp. 1179-1180
    • Hamamoto, T.1    Noguchi, T.2    Midorikawa, Y.3
  • 2
    • 0015244537 scopus 로고
    • Thymidine phosphorylase from Escherichia coli: Properties and kinetics
    • Schwartz, M. (1971). Thymidine phosphorylase from Escherichia coli: properties and kinetics. Eur. J. Biochem. 21, 191-198.
    • (1971) Eur. J. Biochem. , vol.21 , pp. 191-198
    • Schwartz, M.1
  • 3
    • 0016812652 scopus 로고
    • Purification and properties of thymidine phosphorylase from Salmonella typhimurium
    • Blank, J.G. & Hoffee, P.A. (1975). Purification and properties of thymidine phosphorylase from Salmonella typhimurium. Arch. Biochem. Biophys. 168, 259-265.
    • (1975) Arch. Biochem. Biophys. , vol.168 , pp. 259-265
    • Blank, J.G.1    Hoffee, P.A.2
  • 4
    • 0022345955 scopus 로고
    • Kinetic studies of thymidine phosphorylase from mouse liver
    • Iltzch, M.H., el Kouni, M.H. & Cha, S. (1985). Kinetic studies of thymidine phosphorylase from mouse liver. Biochemistry 24, 6799-6807.
    • (1985) Biochemistry , vol.24 , pp. 6799-6807
    • Iltzch, M.H.1    El Kouni, M.H.2    Cha, S.3
  • 5
    • 0025184556 scopus 로고
    • Purification and characterization of uridine and thymidine phosphorylase from Lactobacillus casei
    • Avraham, Y., Grossowicz, N. & Yashphe, J. (1990). Purification and characterization of uridine and thymidine phosphorylase from Lactobacillus casei. Biochim. Biophys. Acta 1040, 287-293.
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 287-293
    • Avraham, Y.1    Grossowicz, N.2    Yashphe, J.3
  • 6
    • 0025160874 scopus 로고
    • Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 Å resolution
    • Walter, M.R. et al., & Ealick, S.E. (1990). Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 Å resolution. J. Biol. Chem. 265 (23), 14016-14022.
    • (1990) J. Biol. Chem. , vol.265 , Issue.23 , pp. 14016-14022
    • Walter, M.R.1    Ealick, S.E.2
  • 7
    • 0032516763 scopus 로고    scopus 로고
    • Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase
    • Pugmire, M.J., Cook, W.J., Jasanoff, A., Walter, M.R. & Ealick, S.E. (1998). Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J. Mol. Biol. 281, 285-299.
    • (1998) J. Mol. Biol. , vol.281 , pp. 285-299
    • Pugmire, M.J.1    Cook, W.J.2    Jasanoff, A.3    Walter, M.R.4    Ealick, S.E.5
  • 8
    • 0025777309 scopus 로고
    • Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenase
    • Gerstein, M. & Chothia, C. (1991). Analysis of protein loop closure: two types of hinges produce one motion in lactate dehydrogenase. J. Mol. Biol. 220, 133-149.
    • (1991) J. Mol. Biol. , vol.220 , pp. 133-149
    • Gerstein, M.1    Chothia, C.2
  • 9
    • 0027438949 scopus 로고
    • Domain closure in lactoferin: Two hinges produce a see-saw motion between alternative close-packed interfaces
    • Gerstein, M., Anderson, B.F., Norris, G.E., Baker, E.N., Lesk, A.M. & Chothia, C. (1993). Domain closure in lactoferin: two hinges produce a see-saw motion between alternative close-packed interfaces. J. Mol. Biol. 234, 357-372.
    • (1993) J. Mol. Biol. , vol.234 , pp. 357-372
    • Gerstein, M.1    Anderson, B.F.2    Norris, G.E.3    Baker, E.N.4    Lesk, A.M.5    Chothia, C.6
  • 10
    • 13144272751 scopus 로고    scopus 로고
    • Cloning, expression, and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus
    • in press
    • Zhou, M., Pugmire, M. J., Vuong, B.Q. & Ealick, S.E. (1998). Cloning, expression, and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. Acta Cryst. D, in press.
    • (1998) Acta Cryst. D
    • Zhou, M.1    Pugmire, M.J.2    Vuong, B.Q.3    Ealick, S.E.4
  • 11
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparison of atomic coordinates
    • Wriggers, W. & Schulten, K. (1997). Protein domain movements: detection of rigid domains and visualization of hinges in comparison of atomic coordinates. Proteins 29, 1-14.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 13
    • 0028330140 scopus 로고
    • Characterization of interactions and metal ion binding sites in proteins
    • Jernigan, R., Raghunathan, G. & Bahar, I. (1994). Characterization of interactions and metal ion binding sites in proteins. Curr. Opin. Struct. Biol. 4, 256-263.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 256-263
    • Jernigan, R.1    Raghunathan, G.2    Bahar, I.3
  • 14
    • 0032546620 scopus 로고    scopus 로고
    • Calf spleen purine nucleoside phosphorylase complexed with substrtaes and substrate analogues
    • Mao, C., Cook, W.J., Zhou, M., Federov, A., Almo, S.C. & Ealick, S.E. (1998). Calf spleen purine nucleoside phosphorylase complexed with substrtaes and substrate analogues. Biochemistry 37, 7135-7146.
    • (1998) Biochemistry , vol.37 , pp. 7135-7146
    • Mao, C.1    Cook, W.J.2    Zhou, M.3    Federov, A.4    Almo, S.C.5    Ealick, S.E.6
  • 15
    • 0030817010 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase 2. Catalytic mechanism
    • Erion, M.D., et al., & Ealick, S.E. (1997). Purine nucleoside phosphorylase 2. Catalytic mechanism. Biochemistry 36, 11725-11734.
    • (1997) Biochemistry , vol.36 , pp. 11725-11734
    • Erion, M.D.1    Ealick, S.E.2
  • 16
    • 0002548426 scopus 로고
    • Structure and conformational properties of bases, furanose sugars and phosphate groups
    • (Cantor, C.R., ed.) Springer-Verlag, New York
    • Saenger, W. (1984). Structure and conformational properties of bases, furanose sugars and phosphate groups. In Principles of Nucleic Acid Structure. (Cantor, C.R., ed.) pp. 51-104. Springer-Verlag, New York.
    • (1984) Principles of Nucleic Acid Structure , pp. 51-104
    • Saenger, W.1
  • 17
    • 0029120977 scopus 로고
    • Structural characterization of thymidine phosphorylase from human placenta
    • Miyadera, K., et al., & Akiyama, S. (1995). Structural characterization of thymidine phosphorylase from human placenta. Biochem. Biophys. Res. Commun. 212 (3), 1040-1045.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , Issue.3 , pp. 1040-1045
    • Miyadera, K.1    Akiyama, S.2
  • 18
    • 0026719635 scopus 로고
    • A novel glial growth inhibitory factor, gliostatin, derived from neurofibroma
    • Asai, K., et al., & Kato, T. (1992). A novel glial growth inhibitory factor, gliostatin, derived from neurofibroma. J. Neurochem. 59, 307-317.
    • (1992) J. Neurochem. , vol.59 , pp. 307-317
    • Asai, K.1    Kato, T.2
  • 19
    • 0026600296 scopus 로고
    • Stimulation of 5-fluorouracil metabolic activation by interferon-α in human colon carcinoma cells
    • Schwartz, E.L., Hoffman, M., O'Connor, C.J. & Wadler, S. (1992). Stimulation of 5-fluorouracil metabolic activation by interferon-α in human colon carcinoma cells. Biochem. Biophys. Res. Commun. 182, 1232-1239.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1232-1239
    • Schwartz, E.L.1    Hoffman, M.2    O'Connor, C.J.3    Wadler, S.4
  • 20
    • 0029156623 scopus 로고
    • The correlation of thymidine phosphorylase activity with the expression of interleukin 1α, interferon α and interferon γ in human colorectal carcinoma
    • Takebayashi, Y., et al., & Aikou, T. (1995). The correlation of thymidine phosphorylase activity with the expression of interleukin 1α, interferon α and interferon γ in human colorectal carcinoma. Cancer Lett. 95, 57-62.
    • (1995) Cancer Lett. , vol.95 , pp. 57-62
    • Takebayashi, Y.1    Aikou, T.2
  • 21
    • 0029021896 scopus 로고
    • The expression of thymidine phosphorylase and thrombomodulin in human colorectal carcinomas
    • Takebayashi, Y., et al., & Aikou, T. (1995). The expression of thymidine phosphorylase and thrombomodulin in human colorectal carcinomas. Cancer Lett. 92, 1-7.
    • (1995) Cancer Lett. , vol.92 , pp. 1-7
    • Takebayashi, Y.1    Aikou, T.2
  • 22
    • 0028951104 scopus 로고
    • Expression of platelet-derived endothelial cell growth factor/thymidine phosphorylase in human breast cancer
    • Toi, M., Hoshina, S., Taniguchi, T., Yamamoto, Y., Ishitsuka, H. & Tominaga, T. (1995). Expression of platelet-derived endothelial cell growth factor/thymidine phosphorylase in human breast cancer, Intl J. Cancer 64, 79-82.
    • (1995) Intl J. Cancer , vol.64 , pp. 79-82
    • Toi, M.1    Hoshina, S.2    Taniguchi, T.3    Yamamoto, Y.4    Ishitsuka, H.5    Tominaga, T.6
  • 23
    • 8944222602 scopus 로고
    • Platelet derived endothelial cell growth factor/thymidine phosphorylase is elevated in bladder cancer
    • Fox, S., et al., & Dickinson, A. (1995). Platelet derived endothelial cell growth factor/thymidine phosphorylase is elevated in bladder cancer. Proc. Am. Urological Assoc. J. Urol. 153, Supplement, p. 521 A.
    • (1995) Proc. Am. Urological Assoc. J. Urol. , vol.153 , Issue.SUPPL.
    • Fox, S.1    Dickinson, A.2
  • 24
    • 0031029591 scopus 로고    scopus 로고
    • Platelet-derived endothelial cell growth factor (thymidine phosphorylase) expression in lung cancer
    • Giatromanolaki, A., et al., & Gatter, K.C. (1997). Platelet-derived endothelial cell growth factor (thymidine phosphorylase) expression in lung cancer. J. Pathol. 181, 196-199.
    • (1997) J. Pathol. , vol.181 , pp. 196-199
    • Giatromanolaki, A.1    Gatter, K.C.2
  • 25
    • 0020037313 scopus 로고
    • 5-Benzylacyclouridine and 5-benzyloxybenzylacyclouridine, potent inhibitors of uridine phosphorylase
    • Niedzwicki, J.G., Chu, S.H., el Kouni, M.H., Rowe, E.G. & Sungman, C. (1982). 5-Benzylacyclouridine and 5-benzyloxybenzylacyclouridine, potent inhibitors of uridine phosphorylase. Biochem. Pharmacol. 31, 1857-1861.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 1857-1861
    • Niedzwicki, J.G.1    Chu, S.H.2    El Kouni, M.H.3    Rowe, E.G.4    Sungman, C.5
  • 26
    • 0018842146 scopus 로고
    • Specificity of pyrimidine nucleoside phosphorylase and the phosphorolysis of 5-fluoro-2′-deoxyuridine
    • Woodman, P.W., Sarrif, A.M. & Heidelberger, C. (1980). Specificity of pyrimidine nucleoside phosphorylase and the phosphorolysis of 5-fluoro-2′-deoxyuridine. Cancer Res. 50, 507-511.
    • (1980) Cancer Res. , vol.50 , pp. 507-511
    • Woodman, P.W.1    Sarrif, A.M.2    Heidelberger, C.3
  • 27
    • 0029100420 scopus 로고
    • Increased sensitivity to the prodrug 5′-deoxy-5-fluorouridine and modulation of 5-fluoro-2′-deoxyuridine sensitivity in MCF-7 cells transfected with thymidine phosphorylase
    • Patterson, A.V., et al., & Harris, A.L. (1995). Increased sensitivity to the prodrug 5′-deoxy-5-fluorouridine and modulation of 5-fluoro-2′-deoxyuridine sensitivity in MCF-7 cells transfected with thymidine phosphorylase. Brit. J. Cancer 72, 669-675.
    • (1995) Brit. J. Cancer , vol.72 , pp. 669-675
    • Patterson, A.V.1    Harris, A.L.2
  • 28
    • 0018906314 scopus 로고
    • Comparison of pharmacokinetics of 5-fluorouracil with concurrent thymidine infusions in a phase I trial
    • Kirkwood, J.M., Ensminger, W., Rosowsky, A., Papathanasopoulos, N. & Frei, E. (1980). Comparison of pharmacokinetics of 5-fluorouracil with concurrent thymidine infusions in a phase I trial. Cancer Res. 40, 107-113.
    • (1980) Cancer Res. , vol.40 , pp. 107-113
    • Kirkwood, J.M.1    Ensminger, W.2    Rosowsky, A.3    Papathanasopoulos, N.4    Frei, E.5
  • 29
    • 0029645281 scopus 로고
    • High-resolution macromolecular structure determination using CCD detectors and synchrotron radiation
    • Walter, R.L., et al., & Ealick, S.E. (1995). High-resolution macromolecular structure determination using CCD detectors and synchrotron radiation. Structure 3, 835-844.
    • (1995) Structure , vol.3 , pp. 835-844
    • Walter, R.L.1    Ealick, S.E.2
  • 31
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on patterson correlation refinement
    • Brünger, A.T. (1990). Extension of molecular replacement: a new search strategy based on patterson correlation refinement. Acta Cryst. A 46, 46-57.
    • (1990) Acta Cryst. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 33
    • 0028797896 scopus 로고
    • The direct rotation function: Rotational patterson correlation search applied to molecular replacement
    • DeLano, W.L. & Brünger, A.T. (1995). The direct rotation function: rotational patterson correlation search applied to molecular replacement. Acta Cryst. D 51, 740-748.
    • (1995) Acta Cryst. D , vol.51 , pp. 740-748
    • DeLano, W.L.1    Brünger, A.T.2
  • 35
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin, C. & Bohacek, R.S. (1997). QXP: powerful, rapid computer algorithms for structure-based drug design. J. Comput. Aided Mol. Des. 11, 333-344.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 333-344
    • McMartin, C.1    Bohacek, R.S.2
  • 36
    • 84986437005 scopus 로고
    • Macromodel - An integrated software system for modeling organic and bioorganic molecules using molecular mechanics
    • Mohamadi, F., et al., & Still, W.C. (1990). Macromodel - an integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J. Comput. Chem. 11, 440-467.
    • (1990) J. Comput. Chem. , vol.11 , pp. 440-467
    • Mohamadi, F.1    Still, W.C.2
  • 37
    • 0021757436 scopus 로고
    • A new force field for molecular mechanical simulation of nucleic acids and proteins
    • Weiner, S.J., et al., & Weiner, P. (1984). A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106, 765-784.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 765-784
    • Weiner, S.J.1    Weiner, P.2
  • 38
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S.J., Kollman, P.A., Nguyen, D.T. & Case, D.A. (1986). An all atom force field for simulations of proteins and nucleic acids. J. Comp. Chem. 7, 230-252.
    • (1986) J. Comp. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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