Affordable Access

deepdyve-link
Publisher Website

One century of ConA and 40 years of ConBr research: A structural review.

Authors
  • Cavada, Benildo Sousa1
  • Osterne, Vinicius Jose Silva2
  • Lossio, Claudia Figueiredo2
  • Pinto-Junior, Vanir Reis2
  • Oliveira, Messias Vital2
  • Silva, Mayara Torquato Lima2
  • Leal, Rodrigo Bainy3
  • Nascimento, Kyria Santiago4
  • 1 BioMol-Lab, Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil. Electronic address: [email protected] , (Brazil)
  • 2 BioMol-Lab, Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil. , (Brazil)
  • 3 Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil. , (Brazil)
  • 4 BioMol-Lab, Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil. Electronic address: [email protected] , (Brazil)
Type
Published Article
Journal
International journal of biological macromolecules
Publication Date
Aug 01, 2019
Volume
134
Pages
901–911
Identifiers
DOI: 10.1016/j.ijbiomac.2019.05.100
PMID: 31108148
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Lectins are proteins that can bind specifically and reversibly to carbohydrates. This capacity gives lectins multiple biological roles and biotechnological applications. Although lectins can be found in all organisms, plant lectins, especially legume lectins, are undoubtedly the most thoroughly studied. Among legume lectins, the lectin from Canavalia ensiformis (ConA) and Canavalia brasiliensis (ConBr), both from Diocleinae subtribe, are two of the most well-known lectins. It has been 100 years since the first report of ConA and 40 years since the first report of ConBr, making 2019 an important year for lectinology. Structural data of these lectins in combination with biological activity tests clearly indicate that even a small shift in amino acid sequence can affect the tertiary and quaternary structures, consequently affecting the biological activity of these proteins. It is in this context that the present paper aims to review the structural data of ConA and ConBr, focusing on the primary structure, crystallography, tertiary and quaternary structures of these lectins, as well as their binding sites. This paper also expands the structural data by employing molecular dynamics to evaluate carbohydrate-binding properties and structural stability. It is anticipated that these data will increase knowledge about the structure-function relationships of these proteins. Copyright © 2019 Elsevier B.V. All rights reserved.

Report this publication

Statistics

Seen <100 times