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Volumn 49, Issue 9, 2010, Pages 2058-2067

Conformational states of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC SITES; CONFORMATIONAL STATE; DEUTERIUM EXCHANGE; DYNAMIC MOTIONS; FOURIER TRANSFORM ION CYCLOTRON RESONANCE MASS SPECTROMETRY; HIGH RESOLUTION; HOMOTRIMERS; IMMUCILLIN-H; INOSINE; KINETIC ANALYSIS; MICHAELIS COMPLEX; PEPTIDE AMIDES; PROTEIN CONFORMATION; PROTEIN DYNAMICS; PURINE NUCLEOSIDE PHOSPHORYLASE; SEDIMENTATION RATES; STRONG BINDING; TRANSITION STATE; TRANSITION-STATE ANALOGUES;

EID: 77749337724     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902041j     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 84919573117 scopus 로고
    • Nucleoside-phosphorylase deficiency in a child with severly defective T-cell immunity and normal B-cell immunity
    • Giblett, E. R., Ammann, A. J., Wara, D. W., Sandman, R., and Diamond, L. K. (1975) Nucleoside-phosphorylase deficiency in a child with severly defective T-cell immunity and normal B-cell immunity, Lancet 1, 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
  • 3
    • 2442729131 scopus 로고
    • Isolation and characterization of purine-nucleoside phosphorylasedeficient T-lymphoma cells and secondary mutants with altered ribonucleotide reductase: Genetic model for immunodeficiency disease
    • Ullman, B., Gudas, L. J., Clift, S. M., and Martin, D. W., Jr. (1979) Isolation and characterization of purine-nucleoside phosphorylasedeficient T-lymphoma cells and secondary mutants with altered ribonucleotide reductase: Genetic model for immunodeficiency disease, Proc. Natl. Acad. Sci. U.S.A. 76, 1074-1078.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 1074-1078
    • Ullman, B.1    Gudas, L.J.2    Clift, S.M.3    Martin Jr., D.W.4
  • 4
    • 35048849848 scopus 로고    scopus 로고
    • Forodesine (BCX-1777, immucillin H) - A new purine nucleoside analogue: Mechanism of action and potential clinical application
    • DOI 10.2174/138955707781662636
    • 4. Korycka, A., Blonski, J. Z., and Robak, T. (2007) Forodesine (BCX-1777, Immucillin H) - a new purine nucleoside analogue: Mechanism of action and potential clinical application. Mini Rev. Med. Chem. 7, 976-983. (Pubitemid 47554785)
    • (2007) Mini-Reviews in Medicinal Chemistry , vol.7 , Issue.9 , pp. 976-983
    • Korycka, A.1    Blonski, J.Z.2    Robak, T.3
  • 5
    • 0027729453 scopus 로고
    • Purine nucleoside Phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction
    • Kline, P. C., and Schramm, V. L. (1993) Purine nucleoside Phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction. Biochemistry 32, 13212-13219.
    • (1993) Biochemistry , vol.32 , pp. 13212-13219
    • Kline, P.C.1    Schramm, V.L.2
  • 6
    • 0037817418 scopus 로고    scopus 로고
    • Exploring structure-activity relationships of transition state analogues of human purine nucleoside phosphorylase
    • DOI 10.1021/jm030145r
    • 6. Evans, G. B., Furneaux, R. H., Lewandowicz, A., Schramm, V. L., and Tyler, P. C. (2003) Exploring structure-activity relationships of transition state analogues of human purine nucleoside Phosphorylase. J. Med. Chem. 46, 3412-3423. (Pubitemid 36842425)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.15 , pp. 3412-3423
    • Evans, G.B.1    Furneaux, R.H.2    Lewandowicz, A.3    Schramm, V.L.4    Tyler, P.C.5
  • 7
    • 1042299983 scopus 로고    scopus 로고
    • Transition State Analysis for Human and Plasmodium falciparum Purine Nucleoside Phosphorylases
    • DOI 10.1021/bi0359123
    • 7. Lewandowicz, A., and Schramm, V. L. (2004) Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases. Biochemistry 43, 1458-1468. (Pubitemid 38200551)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1458-1468
    • Lewandowicz, A.1    Schramm, V.L.2
  • 8
    • 34250205219 scopus 로고    scopus 로고
    • Acyclic ribooxacarbenium ion mimics as transition state analogues of human and malarial purine nucleoside phosphorylases
    • DOI 10.1021/ja071087s
    • 8. Taylor, E. A., Clinch, K., Kelly, P. M., Li, L., Evans, G. B., Tyler, P. C., and Schramm, V. L. (2007) Acyclic ribooxacarbenium ion mimics as transition state analogues of human and malarial purine nucleoside phosphorylases. J. Am. Chem. Soc. 129, 6984-6985. (Pubitemid 46903249)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.22 , pp. 6984-6985
    • Taylor, E.A.1    Clinch, K.2    Kelly, P.M.3    Li, L.4    Evans, G.B.5    Tyler, P.C.6    Schramm, V.L.7
  • 9
    • 0020483829 scopus 로고
    • Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution
    • Wagner, G., and Wuthrich, K. (1982) Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. J. Mol. Biol. 160, 343-361.
    • (1982) J. Mol. Biol. , vol.160 , pp. 343-361
    • Wagner, G.1    Wuthrich, K.2
  • 10
    • 0007501806 scopus 로고
    • Hydrogen/deuterium exchange electrospray ionization mass spectrometry: A method for probing protein conformational changes in solution
    • 10. Katta, V., and Chait, B. T. (1993) Hydrogen/deuterium exchange electrospray ionization mass spectrometry: A method for probing protein conformational changes in solution. J. Am. Chem. Soc. 115, 6317-6321. (Pubitemid 23954706)
    • (1993) Journal of the American Chemical Society , vol.115 , Issue.14 , pp. 6317-6321
    • Katta, V.1    Chait, B.T.2
  • 11
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • 11. Zhang, Z., and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation, Protein Sci. 2, 522-531. (Pubitemid 23119303)
    • (1993) Protein Science , vol.2 , Issue.4 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 12
    • 0030992108 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase
    • DOI 10.1021/bi963065g
    • 12. Wang, F., Blanchard, J. S., and Tang, X. J. (1997) Amide hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of E. coli dihydropicolinate reductase. Biochemistry 36, 3755-3759. (Pubitemid 27154694)
    • (1997) Biochemistry , vol.36 , Issue.13 , pp. 3755-3759
    • Wang, F.1    Blanchard, J.S.2    Tang, X.-J.3
  • 13
    • 0033473730 scopus 로고    scopus 로고
    • Advances in protein hydrogen exchange by mass spectrometry
    • DOI 10.1016/S1044-0305(99)00060-4, PII S1044030599000604
    • 13. Woodward, C. (1999) Advances in protein hydrogen exchange by mass spectrometry. J. Am. Soc. Mass Spectrom. 10, 672-674. (Pubitemid 34498690)
    • (1999) Journal of the American Society for Mass Spectrometry , vol.10 , Issue.8 , pp. 672-674
    • Woodward, C.1
  • 14
    • 34249008107 scopus 로고    scopus 로고
    • Application of hydrogen/deuterium exchange mass spectrometry to study protein tyrosine phosphatase dynamics, ligand binding, and substrate specificity
    • DOI 10.1016/j.ymeth.2007.02.020, PII S1046202307000308, Emerging New Techniques for Studying Protein Phosphatases
    • 14. Zhou, B., and Zhang, Z. Y. (2007) Application of hydrogen/deuterium exchange mass spectrometry to study protein tyrosine phosphatase dynamics, ligand binding, and substrate specificity. Methods 42, 221-233. (Pubitemid 46783583)
    • (2007) Methods , vol.42 , Issue.3 , pp. 227-233
    • Zhou, B.1    Zhang, Z.-Y.2
  • 15
    • 0028149245 scopus 로고
    • Analytical ultracentrifugation of complex macromolecular systems
    • DOI 10.1021/bi00249a001
    • 15. Hansen, J. C., Lebowitz, J., and Demeler, B. (1994) Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 33, 13155-13163. (Pubitemid 24373229)
    • (1994) Biochemistry , vol.33 , Issue.45 , pp. 13155-13163
    • Hansen, J.C.1    Lebowitz, J.2    Demeler, B.3
  • 16
    • 0001209134 scopus 로고    scopus 로고
    • Analytical ultracentrifugation as a contemporary biomolecular research tool
    • Cole, J. L., and Hansen, J. C. (1999) Analytical ultracentrifugation as a contemporary biomolecular research tool. J. Biomol. Tech. 10, 163-174.
    • (1999) J. Biomol. Tech. , vol.10 , pp. 163-174
    • Cole, J.L.1    Hansen, J.C.2
  • 17
    • 35448971602 scopus 로고    scopus 로고
    • A brief introduction to the analytical ultracentrifugation of proteins for beginners
    • (Scott, D. J., Harding, S. E., and Rowe, A. J., Eds.) Royal Society of Chemistry, Cambridge, U.K.
    • Scott, D. J., and Schuck, P. (2005) A brief introduction to the analytical ultracentrifugation of proteins for beginners. In Analytical Ultracentrifugation (Scott, D. J., Harding, S. E., and Rowe, A. J., Eds.) pp 1-25, Royal Society of Chemistry, Cambridge, U.K.
    • (2005) Analytical Ultracentrifugation , pp. 1-25
    • Scott, D.J.1    Schuck, P.2
  • 18
    • 0003268964 scopus 로고
    • A differential ultracentrifuge technique for measuring small changes in sedimentation coefficients
    • Richards, E. G., and Schachman, H. K. (1957) A differential ultracentrifuge technique for measuring small changes in sedimentation coefficients. J. Am. Chem. Soc. 79, 5234-5235.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5234-5235
    • Richards, E.G.1    Schachman, H.K.2
  • 19
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ultracentrifugation: Sedimentation velocity and sedimentation equilibrium
    • Cole, J. L., Lary, J. W., Moody, T. P., and Laue, T. M. (2008) Analytical ultracentrifugation: Sedimentation velocity and sedimentation equilibrium. Methods Cell Biol. 84, 143-179.
    • (2008) Methods Cell Biol. , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.P.3    Laue, T.M.4
  • 20
    • 67049158432 scopus 로고    scopus 로고
    • Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside Phosphorylase
    • Edwards, A. A., Mason, J. M., Clinch, K., Tyler, P. C., Evans, G. B., and Schramm, V. L. (2009) Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside Phosphorylase. Biochemistry 48, 5226-5238.
    • (2009) Biochemistry , vol.48 , pp. 5226-5238
    • Edwards, A.A.1    Mason, J.M.2    Clinch, K.3    Tyler, P.C.4    Evans, G.B.5    Schramm, V.L.6
  • 23
    • 60649094922 scopus 로고    scopus 로고
    • Fast reversed-phase liquid chromatography to reduce back exchange and increase throughput in H/D exchange monitored by FT-ICR mass spectrometry
    • Zhang, H., Bou-Assaf, G. M., Emmett, M. R., and Marshall, A. G. (2009) Fast reversed-phase liquid chromatography to reduce back exchange and increase throughput in H/D exchange monitored by FT-ICR mass spectrometry. J. Am. Soc. Mass Spectrom. 20, 520-524.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 520-524
    • Zhang, H.1    Bou-Assaf, G.M.2    Emmett, M.R.3    Marshall, A.G.4
  • 24
    • 0000178042 scopus 로고
    • Micro-electrospray MS, ultra-high-sensitivity analysis of peptides and proteins
    • Emmett, M. R., and Caprioli, R. M. (1994) Micro-electrospray MS, ultra-high-sensitivity analysis of peptides and proteins. J. Am. Soc. Mass Spectrom. 5, 605-613.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 605-613
    • Emmett, M.R.1    Caprioli, R.M.2
  • 25
    • 57449107282 scopus 로고    scopus 로고
    • Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/ deuterium exchange monitored by fourier transform ion cyclotron resonance mass spectrometry
    • Zhang, H., Kazazic, S., Schaub. T. M., Tipton, J. D., Emmett, M. R., and Marshall, A. G. (2008) Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/ deuterium exchange monitored by fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 80, 9034-9041.
    • (2008) Anal. Chem. , vol.80 , pp. 9034-9041
    • Zhang, H.1    Kazazic, S.2    Schaub, T.M.3    Tipton, J.D.4    Emmett, M.R.5    Marshall, A.G.6
  • 26
    • 44949150382 scopus 로고    scopus 로고
    • High-performance mass spectrometry: Fourier transform ion cyclotron resonance at 14.5 Tesla
    • DOI 10.1021/ac800386h
    • 26. Schaub, T. M., Hendrickson, C. L., Horning, S., Quinn, J. P., Senko, M. W., and Marshall, A. G. (2008) High performance mass spectrometry: Fourier transform ion cyclotron resonance at 14.5 Tesla. Anal. Chem. 80, 3985-3990. (Pubitemid 351812746)
    • (2008) Analytical Chemistry , vol.80 , Issue.11 , pp. 3985-3990
    • Schaub, T.M.1    Hendrickson, C.L.2    Horning, S.3    Quinn, J.P.4    Senko, M.W.5    Marshall, A.G.6
  • 27
    • 0030801864 scopus 로고    scopus 로고
    • Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR
    • 27. Zhang, Z., Li, W., Logan, T. M., Li, M., and Marshall, A. G. (1997) Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR. Protein Sci. 6, 2203-2217. (Pubitemid 27449300)
    • (1997) Protein Science , vol.6 , Issue.10 , pp. 2203-2217
    • Zhang, Z.1    Li, W.2    Logan, T.M.3    Li, M.4    Marshall, A.G.5
  • 28
    • 0020610472 scopus 로고
    • Synthesis of "9-deazaguanosine" and other new pyrrolo[3,2-d]pyrimidine C-nucleosides
    • Lim, M., Ren, Y., Otter, B. A., and Klein, R. S. (1983) Synthesis of "9-deazaguanosine" and other new pyrrolo[3,2-d]pyrimidine C-nucleosides. J. Org. Chem. 48, 780-788.
    • (1983) J. Org. Chem. , vol.48 , pp. 780-788
    • Lim, M.1    Ren, Y.2    Otter, B.A.3    Klein, R.S.4
  • 30
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • 30. Marshall, A. G., Hendrickson, C. L., and Jackson, G. S. (1998) Fourier transform ion cyclotron resonance mass spectrometry: A primer. Mass Spectrom. Rev. 17, 1-35. (Pubitemid 128629493)
    • (1998) Mass Spectrometry Reviews , vol.17 , Issue.1 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 31
    • 0036558157 scopus 로고    scopus 로고
    • Scaling MS plateaus with high-resolution FT-ICRMS
    • Marshall, A. G., Hendrickson, C. L., and Shi, S. D. H. (2002) Scaling MS plateaus with high-resolution FT-ICRMS. Anal. Chem. 74, 253A-259A.
    • (2002) Anal. Chem. , vol.74
    • Marshall, A.G.1    Hendrickson, C.L.2    Shi, S.D.H.3
  • 32
    • 31544456090 scopus 로고    scopus 로고
    • Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase
    • DOI 10.1021/jp051277u
    • 32. Nunez, S., Wing, C., Antoniou, D., Schramm, V. L., and Schwartz, S. D. (2006) Insight into catalytically relevant correlated motions in human purine nucleoside Phosphorylase. J. Phys. Chem. A 110, 463-472. (Pubitemid 43164637)
    • (2006) Journal of Physical Chemistry A , vol.110 , Issue.2 , pp. 463-472
    • Nunez, S.1    Wing, C.2    Antoniou, D.3    Schramm, V.L.4    Schwartz, S.D.5
  • 33
    • 0032480809 scopus 로고    scopus 로고
    • Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization fourier transform ion cyclotron resonance mass spectrometry
    • DOI 10.1021/bi981481q
    • 33. Wang, F., Li, W., Emmett, M. R., Hendrickson, C. L., Marshall, A. G., Zhang, Y., Wu, L., and Zhang, Z. (1998) Conformational and dynamic changes of yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization fourier transform ion cyclotron resonance mass spectrometry. Biochemistry 37, 15289-15299. (Pubitemid 28515989)
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15289-15299
    • Wang, F.1    Li, W.2    Emmett, M.R.3    Hendrickson, C.L.4    Marshall, A.G.5    Zhang, Y.-L.6    Wu, L.7    Zhang, Z.-Y.8
  • 35
    • 68249090787 scopus 로고    scopus 로고
    • Mapping of the allosteric network in the regulation of α-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: Solution-phase H/D exchange monitored by FT-ICR mass spectrometry
    • Frantom, P. A., Zhang, H., Emmett, M. R., Marshall, A. G., and Blanchard, J. S. (2009) Mapping of the allosteric network in the regulation of α-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: Solution-phase H/D exchange monitored by FT-ICR mass spectrometry. Biochemistry 48, 7457-7464.
    • (2009) Biochemistry , vol.48 , pp. 7457-7464
    • Frantom, P.A.1    Zhang, H.2    Emmett, M.R.3    Marshall, A.G.4    Blanchard, J.S.5
  • 36
    • 0032984921 scopus 로고    scopus 로고
    • Modern applications of analytical ultreacentrifugation
    • Laue, T. M., and Stafford, W. F. (1999) Modern applications of analytical ultreacentrifugation. Annu. Rev. Biophys. Biomol. Struct. 28, 75-100.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 75-100
    • Laue, T.M.1    Stafford, W.F.2
  • 37
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • DOI 10.1016/j.cbpa.2006.08.017, PII S1367593106001244, Analytical Techniques/Mechanisms
    • 37. Howlett, G. J., Minton, A. P., and Rivas, G. (2006) Analytical ultracentrifugation for the study of protein association and assembly. Curr. Opin. Chem. Biol. 10, 430-436. (Pubitemid 44375070)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 38
  • 39
    • 0035838469 scopus 로고    scopus 로고
    • A transition-state analogue reduces protein dynamics in hypoxanthine-guanine phosphoribosyltransferase
    • DOI 10.1021/bi010203f
    • 39. Wang, F., Shi, W., Nieves, E., Angeletti, R. H., Schramm, V. L., and Grubmeyer, C. (2001) A transition state analogue reduces protein dynamics in hypoxanthine-guanine phosphoribosyltransferase. Biochemistry 40, 8043-8054. (Pubitemid 32641201)
    • (2001) Biochemistry , vol.40 , Issue.27 , pp. 8043-8054
    • Wang, F.1    Shi, W.2    Nieves, E.3    Angeletti, R.H.4    Schramm, V.L.5    Grubmeyer, C.6
  • 40
    • 0033819339 scopus 로고    scopus 로고
    • Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange
    • 40. Wang, F., Miles, R. W., Kicska, G., Nieves, E., Schramm, V. L., and Angeletti, R. H. (2000) Immucillin-H binding to purine nucleoside Phosphorylase reduces dynamic solvent exchange. Protein Sci. 9, 1660-1668. (Pubitemid 30745464)
    • (2000) Protein Science , vol.9 , Issue.9 , pp. 1660-1668
    • Wang, F.1    Miles, R.W.2    Kicska, G.3    Nieves, E.4    Schramm, V.L.5    Angeletti, R.H.6
  • 41
    • 0032537481 scopus 로고    scopus 로고
    • One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase
    • DOI 10.1021/bi980658d
    • 41. Miles, R. W., Tyler, P. C., Furneaux, R. H., Bagdassarian, C. K., and Schramm, V. L. (1998) One-third-the-sites transition-state inhibitors for purine nucleoside Phosphorylase. Biochemistry 37, 8615-8621. (Pubitemid 28299598)
    • (1998) Biochemistry , vol.37 , Issue.24 , pp. 8615-8621
    • Miles, R.W.1    Tyler, P.C.2    Furneaux, R.H.3    Bagdassarian, C.K.4    Schramm, V.L.5
  • 42
    • 0032546620 scopus 로고    scopus 로고
    • Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues
    • DOI 10.1021/bi9723919
    • 42. Mao, C., Cook, W. J., Zhou, M., Federov, A. A., Almo, S. C., and Ealick, S. E. (1998) Calf spleen purine nucleoside Phosphorylase complexed with substrates and substrate analogues. Biochemistry 37, 7135-7146. (Pubitemid 28235194)
    • (1998) Biochemistry , vol.37 , Issue.20 , 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


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