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

Plant Mol Biol. 1997 Mar;33(4):691-8. doi: 10.1023/a:1005704616565.

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

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Computer Simulation
  • Galanthus
  • Lectins / chemistry*
  • Lectins / metabolism
  • Mannose / chemistry*
  • Mannose / metabolism
  • Mannose-Binding Lectins*
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Lectins
  • Plant Proteins / chemistry*
  • Plant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Sweetening Agents / chemistry*
  • Sweetening Agents / metabolism
  • Taste / drug effects

Substances

  • Lectins
  • Mannose-Binding Lectins
  • Plant Lectins
  • Plant Proteins
  • Sweetening Agents
  • curculin
  • snowdrop lectin
  • Mannose

Associated data

  • PDB/1MSA