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Glycobiology Advance Access published online on March 27, 2006
Glycobiology, 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
Received January 13, 2006
Revised March 23, 2006
Accepted March 23, 2006

Article

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

Lieven Buts 1 * *, Abel Garcia-Pino 1 *, Lode Wyns 1, and Remy Loris 1

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

* To whom correspondence should be addressed.
Lieven Buts, E-mail: lievbuts{at}vub.ac.be


  Abstract

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.

Keywords: legume lectin/carbohydrate recognition/X-ray crystallography/lectin.

* Both authors contributed equally to this work


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