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Volumn 12, Issue 7, 2003, Pages 1386-1394

Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor

Author keywords

Anisotropy; Catalysis; Model free analysis; NMR; Relaxation measurements

Indexed keywords

4 NITROPHENOL; CATALYTIC ANTIBODY; LIGAND; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY NPN43C9; UNCLASSIFIED DRUG;

EID: 0037634024     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0243303     Document Type: Article
Times cited : (15)

References (38)
  • 3
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A.S., Hinton, D.P., and Byrd, R.A. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117: 7566-7567.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 4
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice, T.C. and Benkovic, S.J. 2000. Chemical basis for enzyme catalysis. Biochemistry 39: 6267-6274.
    • (2000) Biochemistry , vol.39 , pp. 6267-6274
    • Bruice, T.C.1    Benkovic, S.J.2
  • 5
    • 0032500701 scopus 로고    scopus 로고
    • A comparison of the crystallographic structures of two catalytic antibodies with esterase activity
    • Buchbinder, J.L., Stephenson, R.C., Scanlan, T.S., and Fletterick, R.J. 1998. A comparison of the crystallographic structures of two catalytic antibodies with esterase activity. J. Mol. Biol. 282: 1033-1041.
    • (1998) J. Mol. Biol. , vol.282 , pp. 1033-1041
    • Buchbinder, J.L.1    Stephenson, R.C.2    Scanlan, T.S.3    Fletterick, R.J.4
  • 6
    • 0032500555 scopus 로고    scopus 로고
    • Solvation, reorganization energy, and biological catalysis
    • Cannon, W.R. and Benkovic, S.J. 1998. Solvation, reorganization energy, and biological catalysis. J. Biol. Chem. 273: 26257-26260.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26257-26260
    • Cannon, W.R.1    Benkovic, S.J.2
  • 7
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C., and Gronenbom, A.M. 1990. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112: 4989-4991.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenbom, A.M.6
  • 11
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote, J. and Milstein, C. 1994. Conformational isomerism and the diversity of antibodies. Proc. Natl. Acad. Sci. 91: 10370-10374.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 12
    • 0028324575 scopus 로고
    • v fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy
    • v fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy. Biochemistry 33: 3296-3303.
    • (1994) Biochemistry , vol.33 , pp. 3296-3303
    • Freund, C.1    Ross, A.2    Plückthun, A.3    Holak, T.A.4
  • 13
    • 0001468012 scopus 로고
    • Substituent effects on an antibody-catalyzed hydrolysis of phenyl esters: Further evidence for an acyl-antibody intermediate
    • Gibbs, R.A., Benkovic, P.A., Janda, K.D., Lerner, R.A., and Benkovic, S.J. 1992. Substituent effects on an antibody-catalyzed hydrolysis of phenyl esters: Further evidence for an acyl-antibody intermediate. J. Am. Chem. Soc. 114: 3528-3534.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3528-3534
    • Gibbs, R.A.1    Benkovic, P.A.2    Janda, K.D.3    Lerner, R.A.4    Benkovic, S.J.5
  • 14
    • 0032484037 scopus 로고    scopus 로고
    • Crossreactivity, efficiency and catalytic specificity of an esterase-like antibody
    • Gigant, B., Charbonnier, J., Eshhar, Z., Green, B.S., and Knossow, M. 1998. Crossreactivity, efficiency and catalytic specificity of an esterase-like antibody. J. Mol. Biol. 284: 741-750.
    • (1998) J. Mol. Biol. , vol.284 , pp. 741-750
    • Gigant, B.1    Charbonnier, J.2    Eshhar, Z.3    Green, B.S.4    Knossow, M.5
  • 15
    • 0027787894 scopus 로고
    • The importance of not saturating H20 in protein NMR. Application to sensitivity enhancement and NOE measurements
    • Grzesiek, S. and Bax, A. 1993. The importance of not saturating H20 in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115: 12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 16
    • 0023759322 scopus 로고
    • Induction of an antibody that catalyzes the hydrolysis of an amide bond
    • Janda, K.D., Schloeder, D., Benkovic, S.J., and Lerner, R.A. 1988. Induction of an antibody that catalyzes the hydrolysis of an amide bond. Science 241: 1188-1191.
    • (1988) Science , vol.241 , pp. 1188-1191
    • Janda, K.D.1    Schloeder, D.2    Benkovic, S.J.3    Lerner, R.A.4
  • 17
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. and Blevins, R.A. 1994. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 604-613.
    • (1994) J. Biomol. NMR , vol.4 , pp. 604-613
    • Johnson, B.A.1    Blevins, R.A.2
  • 19
    • 0028898288 scopus 로고
    • Detection of a catalytic antibody species acylated at the active site by electrospray mass spectrometry
    • Krebs, J.F., Siuzdak, G., Dyson, H.J., Stewart, J.D., and Benkovic, S.J. 1995. Detection of a catalytic antibody species acylated at the active site by electrospray mass spectrometry. Biochemistry 34: 720-723.
    • (1995) Biochemistry , vol.34 , pp. 720-723
    • Krebs, J.F.1    Siuzdak, G.2    Dyson, H.J.3    Stewart, J.D.4    Benkovic, S.J.5
  • 20
    • 0033197310 scopus 로고    scopus 로고
    • Backbone resonance assignments for the Fv fragment of the catalytic antibody NPN43C9 with bound p-nitrophenol
    • Kroon, G.J.A., Martinez-Yamout, M.A., Krebs, J.F., Chung, J., Dyson, H.J., and Wright, P.E. 1999. Backbone resonance assignments for the Fv fragment of the catalytic antibody NPN43C9 with bound p-nitrophenol. J. Biomol. NMR 15: 83-84.
    • (1999) J. Biomol. NMR , vol.15 , pp. 83-84
    • Kroon, G.J.A.1    Martinez-Yamout, M.A.2    Krebs, J.F.3    Chung, J.4    Dyson, H.J.5    Wright, P.E.6
  • 22
    • 0025730616 scopus 로고
    • At the crossroads of chemistry and immunology: Catalytic antibodies
    • Lerner, R.A., Benkovic, S.J., and Schultz, P.G. 1991. At the crossroads of chemistry and immunology: Catalytic antibodies. Science 252: 659-667.
    • (1991) Science , vol.252 , pp. 659-667
    • Lerner, R.A.1    Benkovic, S.J.2    Schultz, P.G.3
  • 23
    • 0033534360 scopus 로고    scopus 로고
    • Conformational changes affect binding and catalysis by ester-hydrolysing antibodies
    • Lindner, A.B., Eshhar, Z., and Tawfik, D.S. 1999. Conformational changes affect binding and catalysis by ester-hydrolysing antibodies. J. Mol. Biol. 285: 421-430.
    • (1999) J. Mol. Biol. , vol.285 , pp. 421-430
    • Lindner, A.B.1    Eshhar, Z.2    Tawfik, D.S.3
  • 24
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. and Szabo, A. 1982a. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104: 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 25
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • -. 1982b. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104: 4559-4570.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4559-4570
  • 26
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A.M., Akke, M., and Palmer, A.G. 1995. Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J. Mol. Biol. 246: 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 27
    • 0028173040 scopus 로고
    • 1H nuclear magnetic resonance of an antidinitrophenyl spin label antibody
    • 1H nuclear magnetic resonance of an antidinitrophenyl spin label antibody. J. Mol. Biol. 244: 301-318.
    • (1994) J. Mol. Biol. , vol.244 , pp. 301-318
    • Martinez-Yamout, M.1    McConnell, H.M.2
  • 28
    • 0031808658 scopus 로고    scopus 로고
    • Stretching exercises - Flexibility in dihydrofolate reductase catalysis
    • Miller, G.P. and Benkovic, S.J. 1998. Stretching exercises - Flexibility in dihydrofolate reductase catalysis. Chem. Biol. 5: 105-113.
    • (1998) Chem. Biol. , vol.5 , pp. 105-113
    • Miller, G.P.1    Benkovic, S.J.2
  • 29
    • 0035072684 scopus 로고    scopus 로고
    • Anisotropic rotational diffusion in model-free analysis for a ternary-DHFR complex
    • Osborne, M.J. and Wright, P.E. 2001. Anisotropic rotational diffusion in model-free analysis for a ternary-DHFR complex. J. Biomol. NMR 19: 209-230.
    • (2001) J. Biomol. NMR , vol.19 , pp. 209-230
    • Osborne, M.J.1    Wright, P.E.2
  • 30
    • 0038466357 scopus 로고    scopus 로고
    • Palmer, A.G. 2000. ModelFree 4.10. http://cpmcnet.columbia.edu/dept/gsas/biochem/labs/palmer/software.html
    • (2000) ModelFree 4.10
    • Palmer, A.G.1
  • 31
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenár, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 32
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz, J.L. and Brooks III, C.L. 2000. Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase. J. Am. Chem. Soc. 122: 225-231.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks C.L. III2
  • 33
    • 0000791343 scopus 로고
    • Antibody catalysis of difficult chemical transformations
    • Schultz, P.G. and Lerner, R.A. 1993. Antibody catalysis of difficult chemical transformations. Accounts Chem. Res. 26: 391-395.
    • (1993) Accounts Chem. Res. , vol.26 , pp. 391-395
    • Schultz, P.G.1    Lerner, R.A.2
  • 34
    • 0028817877 scopus 로고
    • From molecular diversity to catalysis: Lessons from the immune system
    • -. 1995. From molecular diversity to catalysis: Lessons from the immune system. Science 269: 1835-1842.
    • (1995) Science , vol.269 , pp. 1835-1842
  • 38
    • 0029900275 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects. J. Am. Chem. Soc. 118: 6986-6991.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6986-6991
    • Tjandra, N.1    Szabo, A.2    Bax, A.3


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