International Journal of Molecular Sciences (Dec 2018)

ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

  • Benildo S. Cavada,
  • Vanir R. Pinto-Junior,
  • Vinicius J. S. Osterne,
  • Kyria S. Nascimento

DOI
https://doi.org/10.3390/ijms20010030
Journal volume & issue
Vol. 20, no. 1
p. 30

Abstract

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Lectins are a widely studied group of proteins capable of specific and reversible binding to carbohydrates. Undoubtedly, the best characterized are those extracted from plants of the Leguminosae family. Inside this group of proteins, those from the Diocleinae subtribe have attracted attention, in particular Concanavalin A (ConA), the best-studied lectin of the group. Diocleinae lectins, also called ConA-like lectins, present a high similarity of sequence and three-dimensional structure and are known to present inflammatory, vasoactive, antibiotic, immunomodulatory and antitumor activities, among others. This high similarity of lectins inside the ConA-like group makes it possible to use them to study structure/biological activity relationships by the variability of both carbohydrate specificity and biological activities results. It is in this context the following review aims to summarize the most recent data on the biochemical and structural properties, as well as biological activities, of ConA-like lectins and the use of these lectins as models to study structure/biological activity relationships.

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