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J Struct Biol. 2006 Jun;154(3):280-6. Epub 2006 Apr 21.

Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.

Author information

1
Departamento de Bioquímica e Biologia Molecular--Universidade Federal do Ceará, Brazil.

Abstract

The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.

PMID:
16677825
DOI:
10.1016/j.jsb.2006.03.011
[Indexed for MEDLINE]

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