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

被引:28
|
作者
Barre, A
VanDamme, EJM
Peumans, WJ
Rouge, P
机构
[1] FAC PHARMACEUT SCI, UPR CNRS 9062, INST PHARMACEUT & BIOL STRUCT, F-31062 TOULOUSE, FRANCE
[2] KATHOLIEKE UNIV LEUVEN, LAB PHYTOPATHOL & PLANT PROTECT, B-3001 LOUVAIN, BELGIUM
关键词
sweet proteins; lectins; curculin; molecular modelling; docking; epitopes;
D O I
10.1023/A:1005704616565
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:691 / 698
页数:8
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