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

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 pa...

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Autores principales: Cavada, Benildo S., Pinto-Junior, Vanir R., Osterne, Vinicius J. S., Nascimento, Kyria S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337138/
https://www.ncbi.nlm.nih.gov/pubmed/30577614
http://dx.doi.org/10.3390/ijms20010030
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author Cavada, Benildo S.
Pinto-Junior, Vanir R.
Osterne, Vinicius J. S.
Nascimento, Kyria S.
author_facet Cavada, Benildo S.
Pinto-Junior, Vanir R.
Osterne, Vinicius J. S.
Nascimento, Kyria S.
author_sort Cavada, Benildo S.
collection PubMed
description 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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spelling pubmed-63371382019-01-22 ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships Cavada, Benildo S. Pinto-Junior, Vanir R. Osterne, Vinicius J. S. Nascimento, Kyria S. Int J Mol Sci Review 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. MDPI 2018-12-21 /pmc/articles/PMC6337138/ /pubmed/30577614 http://dx.doi.org/10.3390/ijms20010030 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Cavada, Benildo S.
Pinto-Junior, Vanir R.
Osterne, Vinicius J. S.
Nascimento, Kyria S.
ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title_full ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title_fullStr ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title_full_unstemmed ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title_short ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships
title_sort cona-like lectins: high similarity proteins as models to study structure/biological activities relationships
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337138/
https://www.ncbi.nlm.nih.gov/pubmed/30577614
http://dx.doi.org/10.3390/ijms20010030
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