Publicação: Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant. mutation in ConA-like lectins
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2006-06-01
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Elsevier B.V.
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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 B.V. All rights reserved.
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Journal of Structural Biology. San Diego: Academic Press Inc. Elsevier B.V., v. 154, n. 3, p. 280-286, 2006.
