Probing Carbohydrate-Protein Interactions by High-Resolution NMR Spectroscopy
An important requirement for a detailed understanding of the molecular basis of the interaction of a carbohydrate with its protein receptor is a high-resolution three dimensional structure of the complex. Historically, such structural information has derived from crystallographic studies which can illustrate in detail the precise nature of certain carbohydrate-protein interactions in the solid state (reviewed by Cambillau (1995)). In contrast, few high-resolution structural studies of glycan-protein interactions in solution using nuclear magnetic resonance have been reported. The solution structure of the complex is of importance since a comparison with the solution structure of the free ligand may be more meaningful, and moreover the dynamics of the system are accessible from relaxation time measurements.
KeywordsResonance Assignment Glycosidic Linkage Nuclear Overhauser Effect Carbohydrate Ligand Adjacent Monomer
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- 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.PubMedCrossRefGoogle Scholar
- 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.Google Scholar
- Cambillau, C., 1995, The structural features of carbohydrate-protein interactions revealed by x-ray crystallography, in “New Comprehensive Biochemistry” eds. Neuberger A. and van Deenen, L. L. M. Vol 29a: pp 29–65.Google Scholar
- Clore, G. M. and Gronenborn, A. M., 1982, Theory and applications of the transferred Overhauser effect to the study of the conformations of small ligands bound to proteins, J. Magn. Reson. 48: 402.Google Scholar
- Clore, G. M. and Gronenborn, A. M., 1983, Theory of the time-dependent transferred nuclear Overhauser effect: applications to structural analysis of ligand-protein complexes in solution., J. Magn. Reson. 53: 423.Google Scholar
- 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.Google Scholar
- Low, D. G., Probert, M. A., Embleton, G., Seshadri, K., Field, R. A., Homans, S.W., Windust, J. and Davis, P. J., 1996, Structure of a glycoconjugate in solution and in complex with an antibody Fv fragment, Glycobiology in press.Google Scholar
- Nyholm, P-G., Magnusson, G., Zheng, Z., Norel, R., Binnington-Boyd, B. and Lingwood, C. A., 1996, Two distinct binding sites for globotriaosyl ceramide on verotoxins: identification by molecular modelling and confirmation using deoxy analogues and a new glycolipid receptor for all verotoxins, Chemistry and Biology 3: 263.PubMedCrossRefGoogle Scholar
- Perkins, S. J., 1982, Application of ring current calculations to the protein and transfer RNA, in “Biological Magnetic Resonance” (eds. Berliner, L., and Reuben, J.) Plenum Press, New York. Vol. 4, Chapter 4, pp 193–336.Google Scholar