New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the architecture, binding selectivity and plasticity of the carbohydrate-binding sites of the proteins. New insights into the conformational behaviour of free and protein-bound glycomimetics pave the way for the design of carbohydrate-based therapeutics. Finally, recent progress towards elucidating the influence of glycosylation on peptide conformation will be of key importance to fully understanding the role of carbohydrates in the function of glycopeptides.
Kogelberg
Heide
H
The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park Institute of Medical Research, Harrow, Middlesex, HA1 3UJ, UK. h.kogelberg@imperial.ac.uk
Solís
Dolores
D
Jiménez-Barbero
Jesús
J
D001665:Binding Sites; D040761:Biomimetic Materials / Q000032:analysis / Q000737:chemistry; D002241:Carbohydrates / Q000032:analysis / Q000737:chemistry*; D018604:Epitope Mapping / Q000379:methods*; D006023:Glycoproteins / Q000032:analysis / Q000737:chemistry; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis / Q000737:chemistry*
D002241:Carbohydrates; D006023:Glycoproteins; D046911:Macromolecular Substances; D011506:Proteins