Crystal Structure of a Lectin from Canavalia Maritima (Conm) in Complex with Trehalose and Maltose Reveals Relevant Mutation in Cona-like Lectins.
From: Departamento de Bioquímica e Biologia Molecular — Universidade Federal do Ceará, Brazil.
Journal of structural biology
- Publish Date: Jun 2006
- ISSN: 1047-8477
- Volume: 154
- Issue: 3
- Pages: 280-6
- Medium: Print
- Language: English
- Citation (JAMA): Delatorre Plínio, Rocha Bruno A M, Gadelha Carlos A A, et al. Crystal Structure of a Lectin from Canavalia Maritima (Conm) in Complex with Trehalose and Maltose Reveals Relevant Mutation in Cona-like Lectins.. J. Struct. Biol. Jun 2006;154:280-6
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.
Mesh Headings (Keywords): Binding Sites, Canavalia, Carbohydrates, Concanavalin A, Crystallography, X-Ray, Electrons, Hydrogen Bonding, Lectins, Maltose, Molecular Conformation, Mutation, Protein Conformation, Software, Trehalose
Check for Full Text / PubMed Unique Identifier (PMID): 16677825
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