title: Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.
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.
authors: Departamento de Bioquímica e Biologia Molecular--Universidade Federal do Ceará, Brazil.
authors: Plínio
authors: P
authors: Delatorre
authors: Bruno A M
authors: BA
authors: Rocha
authors: Carlos A A
authors: CA
authors: Gadelha
authors: Tatiane
authors: T
authors: Santi-Gadelha
authors: João B
authors: JB
authors: Cajazeiras
authors: Emmanuel P
authors: EP
authors: Souza
authors: Kyria S
authors: KS
authors: Nascimento
authors: Valder N
authors: VN
authors: Freire
authors: Alexandre H
authors: AH
authors: Sampaio
authors: Walter F
authors: WF
authors: Azevedo
authors: Benildo S
authors: BS
authors: Cavada