A structure of the complex between concanavalin A and methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside reveals two binding modes. 1996

R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
Laboratorium voor Ultrastruktuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 Sint-Genesius-Rode, Belgium. bouckaej@vub.ac.be

The structure of concanavalin A in complex with the trimannoside methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside has been determined in a novel space group. In three of the four subunits of the concanavalin A tetramer, the interactions between the protein and the bound saccharide are essentially identical to those reported previously by other authors (Naismith, J. H., and Field, R. A. (1996) J. Biol. Chem. 271, 972-976). In the fourth subunit, however, the alpha1-->3 linkage has a different conformation, resulting in a different part of the alpha1-->3-linked mannose interacting with essentially the same surface of the protein. Furthermore, significant differences are observed in the quaternary associations of the subunits compared with the saccharide-free structures and other carbohydrate complexes, suggesting that the concanavalin A tetramer is a rather flexible entity.

UI MeSH Term Description Entries
D008362 Mannosides Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with an alcohol to form an acetal. They include both alpha- and beta-mannosides. Mannoside
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D009038 Motion Physical motion, i.e., a change in position of a body or subject as a result of an external force. It is distinguished from MOVEMENT, a process resulting from biological activity. Motions
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003208 Concanavalin A A MANNOSE/GLUCOSE binding lectin isolated from the jack bean (Canavalia ensiformis). It is a potent mitogen used to stimulate cell proliferation in lymphocytes, primarily T-lymphocyte, cultures.
D006860 Hydrogen Bonding A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond
D014312 Trisaccharides Oligosaccharides containing three monosaccharide units linked by glycosidic bonds. Trisaccharide

Related Publications

R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
July 1996, Acta crystallographica. Section D, Biological crystallography,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
December 1995, Carbohydrate research,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
April 2003, Acta crystallographica. Section C, Crystal structure communications,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
May 1986, Journal of molecular biology,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
December 1979, Carbohydrate research,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
September 1986, Carbohydrate research,
R Loris, and D Maes, and F Poortmans, and L Wyns, and J Bouckaert
December 1978, The Journal of biological chemistry,
Copied contents to your clipboard!