Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2829668 | Journal of Structural Biology | 2006 | 7 Pages |
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.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Plínio Delatorre, Bruno A.M. Rocha, Carlos A.A. Gadelha, Tatiane Santi-Gadelha, João B. Cajazeiras, Emmanuel P. Souza, Kyria S. Nascimento, Valder N. Freire, Alexandre H. Sampaio, Walter F. Azevedo Jr., Benildo S. Cavada,