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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• 作者：Plí ; nio Delatorre ; Bruno A.M. Rocha ; Carlos A.A. Gadelha ; Tatiane Santi-Gadelha ; Joã ; o B. Cajazeiras ; Emmanuel P. Souza ; Kyria S. Nascimento ; Valder N. Freire ; Alexandre H. Sampaio ; Walter F.
• 关键词：Lectins ; Canavalia maritima ; Crystal structure ; Mutation
• 刊名：Journal of Structural Biology
• 出版年：2006
• 出版时间：June 2006
• 年：2006
• 卷：154
• 期：3
• 页码：280-286
• 全文大小：593 K

文摘

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.