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