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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Data
2006-06-01
Autores
Delatorre, P.
Rocha, BAM
Gadelha, CAA
Santi-Gadelha, T.
Cajazeiras, J. B.
Souza, E. P.
Nascimento, K. S.
Freire, V. N.
Sampaio, A. H.
Azevedo, W. F.
Título da Revista
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Título de Volume
Editor
Elsevier B.V.
Resumo
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. (c) 2006 Elsevier B.V. All rights reserved.
Descrição
Palavras-chave
lectins, Canavalia maritima, Crystal structure, mutation
Como citar
Journal of Structural Biology. San Diego: Academic Press Inc. Elsevier B.V., v. 154, n. 3, p. 280-286, 2006.