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.
(c) 2006 Elsevier Inc. All rights reserved.
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