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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Computer Simulation
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Galanthus
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Lectins / chemistry*
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Lectins / metabolism
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Mannose / chemistry*
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Mannose / metabolism
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Mannose-Binding Lectins*
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Models, Molecular
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Molecular Sequence Data
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Plant Lectins
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Plant Proteins / chemistry*
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Plant Proteins / metabolism
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
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Sweetening Agents / chemistry*
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Sweetening Agents / metabolism
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Taste / drug effects
Substances
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Lectins
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Mannose-Binding Lectins
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Plant Lectins
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Plant Proteins
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Sweetening Agents
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curculin
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snowdrop lectin
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Mannose