Protein-Carbohydrate Interactions Studied by NMR: From Molecular Recognition to Drug Design
Authors:
- Dolores DiazDDDolores Diaz
- Manuel Alvaro BerbisMBManuel Alvaro Berbis
- Filipa MarceloFMFilipa Marcelo
- Javier CanadaJCJavier Canada
- Jesus Jimenez-BarberoJesus Jimenez-Barbero
Open Access
- 1 December 2012
- journal article
- review article
- Published by Bentham Science Publishers Ltd. in Current Protein & Peptide Science
- Vol. 13 (8) , 816-830
Abstract
Diseases that result from infection are, in general, a consequence of specific interactions between a pathogenic organism and the cells. The study of host-pathogen interactions has provided insights for the design of drugs with therapeutic properties. One area that has proved to be promising for such studies is the constituted by carbohydrates which participate in biological processes of paramount importance. On the one hand, carbohydrates have shown to be information carriers with similar, if not higher, importance than traditionally considered carriers as amino acids and nucleic acids. On the other hand, the knowledge on molecular recognition of sugars by lectins and other carbohydrate-binding proteins has been employed for the development of new biomedical strategies. Biophysical techniques such as X-Ray crystallography and NMR spectroscopy lead currently the investigation on this field. In this review, a description of traditional and novel NMR methodologies employed in the study of sugar-protein interactions is briefly presented in combination with a palette of NMR-based studies related to biologically and/or pharmaceutically relevant applications.Keywords
This publication has 100 references indexed in Scilit:
- Towards a Structural Basis for the Relationship Between Blood Group and the Severity of El Tor CholeraAngewandte Chemie International Edition, 2012
- Targeting glucose metabolism for cancer therapyJournal of Experimental Medicine, 2012
- Structural Basis for the Interaction of Lipopolysaccharide with Outer Membrane Protein H (OprH) from Pseudomonas aeruginosaJournal of Biological Chemistry, 2011
- Saturation Transfer Difference NMR Experiments of Membrane Proteins in Living Cells under HR‐MAS Conditions: The Interaction of the SGLT1 Co‐transporter with Its LigandsChemistry – A European Journal, 2011
- Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3Journal of the American Chemical Society, 2010
- Bioinformatics and molecular modeling in glycobiologyCellular and Molecular Life Sciences, 2010
- Immunological Evidence for Functional Rather than Structural Mimicry by aShigella flexneriY Polysaccharide-Mimetic PeptideClinical and Vaccine Immunology, 2008
- Structure determination of a Galectin‐3–carbohydrate complex using paramagnetism‐based NMR constraintsProtein Science, 2008
- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular SimulationJournal of Chemical Theory and Computation, 2008
- An improved OPLS–AA force field for carbohydratesJournal of Computational Chemistry, 2002