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Comparative Study
. 1997 Mar;33(4):691-8.
doi: 10.1023/a:1005704616565.

Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin

A Barre  1 , E J Van Damme, W J Peumans, P Rougé
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Comparative Study

Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin

A Barre et al. Plant Mol Biol. 1997 Mar.

Abstract

A three-dimensional model of curculin, a sweet-tasting and taste-modifying protein from the fruits of Curculigo latifolia, was built from the X-ray coordinates of GNA, a mannose-binding lectin from snowdrop (Galanthus nivalis). The three mannose-binding sites present in GNA were found in curculin but are devoid of mannose-binding activity as shown by docking experiments performed with mannose. Some regions well exposed on the surface of the three-dimensional model of curculin could act as epitopes responsible for the sweet-tasting properties of this protein.

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