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Glycobiology Advance Access originally published online on March 27, 2006
Glycobiology 2006 16(7):635-640; doi:10.1093/glycob/cwj109
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Structural basis of carbohydrate recognition by a Man({alpha}1-2)Man-specific lectin from Bowringia milbraedii

Lieven Buts1,*, Abel Garcia-Pino*, Lode Wyns and Remy Loris

Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Pleinlaan 2, B-1050 Brussels, Belgium

1 To whom correspondence should be addressed; e-mail: lievbuts{at}vub.ac.be

Received on January 13, 2006; revised on March 23, 2006; accepted on March 23, 2006

The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man({alpha}1-2)Man. In solution, the protein exhibits a dynamic dimer–tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man({alpha}1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219.

Key words: carbohydrate recognition / lectin / legume lectin / X-ray crystallography

* These authors contributed equally to this work.


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