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Article

Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.

Journal of structural biology - 1 Jun 2006

Delatorre Plínio, Rocha Bruno A M, Gadelha Carlos A A, Santi-Gadelha Tatiane, Cajazeiras João B, Souza Emmanuel P, Nascimento Kyria S, Freire Valder N, Sampaio Alexandre H, Azevedo Walter F, Cavada Benildo S

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16677825
DOI: 10.1016/j.jsb.2006.03.011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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