Structure of a glycoconjugate in solution and in complex with an antibody Fv fragment

Glycobiology

Volumn 7, Issue 3, 1997, Pages 373-381

  Low, D G ^a   Probert, M A ^a   Embleton, G ^a   Seshadri, K ^a   Field, R A ^a   Homans, S W ^a   Windust, J ^b   Davis, P J ^b  

^a UNIVERSITY OF ST ANDREWS   (United Kingdom)

^b UNILEVER RESEARCH   (United Kingdom)

Author keywords

Antibody; Estrone; NMR; Ring current shifts

Indexed keywords

GLYCOCONJUGATE;

ANTIGEN BINDING; ARTICLE; DRUG STRUCTURE; IN VITRO STUDY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL;

EID: 0030955161     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.3.373     Document Type: Article

References (27)

1. Arepalli, S.R., Glaudemans, C.P.J., Daves, G.D., Kovac, P. and Bax, A. (1995) Identification of protein-mediated indirect nOe effects in a disaccharide-Fab′ complex by transferred ROESY. J. Magn. Reson. B, 106, 195-198.
2. Asensio, J.L., Cañada, F.J. and Jimenez-Barbero, J. (1995) Studies of the bound conformations of methyl alpha-lactoside and methyl beta-allolactoside to ricin b-chain using transferred NOE experiments in the laboratory and rotating frames, assisted by molecular mechanics and dynamics calculations. Eur. J. Biochem., 233, 618-630.
3. Bax, A., Clore, G.M., Driscoll, P.C., Gronenborn, A.M. Ikura, M. and Kay, L.E. (1990) Practical aspects of proton-carbon-carbon-proton 3-dimensional correlation spectroscopy of C-13-labelled proteins. J. Magn. Reson., 87, 620-627.
4. Bevilacqua, V.L., Thomson, D.S. and Prestegard, J.H. (1990) Conformation of methyl beta-lactoside bound to the ricin-b-chain - interpretation of transferred nuclear Overhauser effects facilitated by spin simulation and selective deuteration. Biochemistry, 29, 5529-5537.
5. Bundle, D.R., Baumann, H., Brisson, J.R., Gagne, S.M., Zdanov, A and Cygler, M. (1994) Solution structure of a trisaccharide-antibody complex -comparison of NMR measurements with a crystal structure. Biochemistry, 33, 5183-5192.
6. Cambillau, C. (1995) The structural features of protein-carbohydrate interactions revealed by x-ray crystallography. In Neuberger, A. and van Deenen, L.L.M. (eds), New Comprehensive Biochemistry, Vol 29a. Elsevier, Amsterdam, pp. 29-65.
7. Conrow, R.B. and Bernstein, S. (1971) Steroid conjugates VI. An improved Koenigs-Knorr synthesis of aryl glucuronides using cadmium carbonate, a new and effective catalyst. J. Org. Chem., 36, 863-870.
8. Forster, M. (1991) Comparison of computational methods for simulating nuclear Overhauser effects in NMR spectroscopy. J. Comp. Chem., 12, 292-300.
9. Glaudemans, C.P.J., Lerner, L., Daves, G.D., Kovac, P., Venable, R. and Bax, A. (1990) Significant conformational changes in an antigenic carbohydrate epitope upon binding to a monoclonal antibody. Biochemistry. 29, 10906-10911.
10. Griesinger, C., and Ernst, R.R. (1987) Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy. J. Magn. Reson., 75, 261-271.
11. Homans, S. W. and Forster, M. (1992) Application of restrained minimization, simulated annealing and molecular dynamics simulations for the conformational analysis of oligosaccharides. Glycobiology, 2, 143-151.
12. London, R.E., Perlman, M.E. and Davis, D.G. (1992) Relaxation matrix analysis of the transferred Overhauser effect for finite exchange rates. J. Magn. Reson., 97, 79-98.
13. Ni, F. (1994) Recent developments in transferred NOE methods. Prog. NMR Spectr., 26, 517-606.
14. Perkins, S.J. (1982) Application of ring current calculations to the protein and transfer RNA. In Berliner, L. and Reuben, J. (eds), Biological Magnetic Resonance, Vol. 4, Chapter 4, Plenum Press, New York, pp. 193-336.
15. Petros, A.M., Kawai, M., Luly, J.R. and Fesik, S.W. (1992) Conformation of two immunosuppresive FK506 analogues when bound to FKBP by isotope-filtered NMR. FEBS Lett., 308, 309-314.
16. Rutherford, T.J. and Homans, S.W. (1994) Restrained vs. free dynamics simulations of oligosaccharides-application to solution dynamics of biantennary and bisected biantennary N-linked glycans. Biochemistry, 33, 9606-9614.
17. Sauter, N.K., Bednarski, M.D., Wurzburg, B.A., Hanson, J.E., Whitesides, G.M., Skehel, J.J. and Wiley, D.C. (1989) Hemagglutinins from two influenza-virus variants bind to sialic-acid derivatives with millimolar dissociation constants - a 500 MHz proton NMR study. Biochemistry, 28, 8388-8396.
18. Scheffler, K., Ernst, B., Katapodis, A., Magnani, J.L., Wang, W.T., Weiseman, R., and Peters, T. (1995) Determination of the bioactive conformation of the carbohydrate ligand in the e-selectin sialyl Lewis(x) complex. Angew. Chem. Int. Ed. Engl., 34, 1841-1844.
19. Sigurskjold, B.W., Altman, E. and Bundle, D.R. (1991) Sensitive titration microcalorimetric study of the binding of salmonella o-antigenic oligosaccharides by a monoclonal antibody. Eur. J. Biochem., 197, 239-246.
20. Sigurskjold, B.W. and Bundle, D.R. (1992) Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a salmonella o-antigen point to hydrophobic interactions in the binding site. J. Biol. Chem., 267, 8371-8376.
21. Torda, A.E., Scheek, R.M. and van Gunsteren, W.F. (1990) Time-averaged nuclear Overhauser effect distance restraints applied to tendamistat. J. Mol. Biol., 214, 223-235.
22. Tropp, J. (1980) Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating internuclear distances. J. Chem. Phys., 72, 6035-6044.
23. Tsou, K-C. and Seligman, A.M. (1953) Synthesis of phenyl β-D-glucopyranoside. J. Am. Chem. Soc., 75, 1042-1044.
24. Vuister, G.W. and Bax, A. (1993) Measurement of two-bond and three-bond proton to methyl carbon J-couplings in proteins uniformly enriched with C13. J. Magn. Reson. B, 102, 228-231.
25. Weber, C., Wider, G., von Freyberg, B., Traber, R., Braun, W., Widmer, H. and WYthrich, K. (1991) The NMR structure of cyclosporine-A bound to cyclophilin in aqueous solution. Biochemistry, 30, 6563-6574.
26. Weimar, T., Harris, S.L., Pitner, J.B., Bock, K. and Pinto, B.M. (1995) Transferred nuclear Overhauser enhancement experiments show that the monoclonal-antibody strep-9 selects a local minimum conformation of a streptococcus group-A trisaccharide-hapten. Biochemistry, 34, 13672-13681.
27. Weimar, T. and Peters, T. (1994) Aleuria aurantia agglutinin recognizes multiple conformations of α-L-Fuc(1-6)-β-D-GlcNAc-OMe. Angew. Chem. Int. Ed. Engl., 33, 88-91.