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

@article{Delatorre2006CrystalSO,
  title={Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.},
  author={Pl{\'i}nio Delatorre and Bruno A M Rocha and Carlos Alberto de Almeida Gadelha and Tatiane Santi-Gadelha and Jo{\~a}o Batista Cajazeiras and Emmanuel Prata de Souza and Kyria Santiago do Nascimento and V. N. Freire and Alexandre Holanda Sampaio and Walter Filgueira de Azevedo and Benildo Sousa Cavada},
  journal={Journal of structural biology},
  year={2006},
  volume={154 3},
  pages={280-6}
}
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… CONTINUE READING

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