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Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin
A Barre1, E J Van Damme, W J Peumans
1Institut de Pharmacologie et Biologie Structurale, UPR CNRS 9062, Faculté des Sciences Pharmaceutiques, Toulouse, France.
Plant Molecular Biology
|March 1, 1997
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.