1ona
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(New page: 200px<br /><applet load="1ona" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ona, resolution 2.35Å" /> '''CO-CRYSTALS OF CONCA...)
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Revision as of 20:54, 20 November 2007
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CO-CRYSTALS OF CONCANAVALIN A WITH METHYL-3,6-DI-O-(ALPHA-D-MANNOPYRANOSYL)-ALPHA-D-MANNOPYRANOSIDE
Overview
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.
About this Structure
1ONA is a Single protein structure of sequence from Canavalia ensiformis with MN and CA as ligands. Full crystallographic information is available from OCA.
Reference
A structure of the complex between concanavalin A and methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside reveals two binding modes., Loris R, Maes D, Poortmans F, Wyns L, Bouckaert J, J Biol Chem. 1996 Nov 29;271(48):30614-8. PMID:8940035
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Categories: Canavalia ensiformis | Single protein | Bouckaert, J. | Loris, R. | Maes, D. | Poortmans, F. | Wyns, L. | CA | MN | Calcium | Glycoprotein | Manganese | Plant lectin | Signal
