The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins
Autor(a) principal: | |
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Data de Publicação: | 1996 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Memórias do Instituto Oswaldo Cruz |
Texto Completo: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761996000600021 |
Resumo: | The carbohydrate-binding specificity of lectins from the seeds of Canavalia maritima and Dioclea grandiflora was studied by hapten-inhibition of haemagglutination using various sugars and sugar derivatives as inhibitors, including N-acetylneuraminic acid and N-acetylmuramic acid. Despite some discrepancies, both lectins exhibited a very similar carbohydrate-binding specificity as previously reported for other lectins from Diocleinae (tribe Phaseoleae, sub-tribe Diocleinae). Accordingly, both lectins exhibited almost identical hydropathic profiles and their three-dimensional models built up from the atomic coordinates of ConA looked very similar. However, docking experiments of glucose and mannose in their monosaccharide-binding sites, by comparison with the ConA-mannose complex used as a model, revealed conformational changes in side chains of the amino acid residues involved in the binding of monosaccharides. These results fully agree with crystallographic data showing that binding of specific ligands to ConA requires conformational chances of its monosaccharide-binding site. |
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Memórias do Instituto Oswaldo Cruz |
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The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectinsCanavalia maritimacarbohydrate-binding specificityDiocleinaeDioclea grandifloralectinsmolecular modellingThe carbohydrate-binding specificity of lectins from the seeds of Canavalia maritima and Dioclea grandiflora was studied by hapten-inhibition of haemagglutination using various sugars and sugar derivatives as inhibitors, including N-acetylneuraminic acid and N-acetylmuramic acid. Despite some discrepancies, both lectins exhibited a very similar carbohydrate-binding specificity as previously reported for other lectins from Diocleinae (tribe Phaseoleae, sub-tribe Diocleinae). Accordingly, both lectins exhibited almost identical hydropathic profiles and their three-dimensional models built up from the atomic coordinates of ConA looked very similar. However, docking experiments of glucose and mannose in their monosaccharide-binding sites, by comparison with the ConA-mannose complex used as a model, revealed conformational changes in side chains of the amino acid residues involved in the binding of monosaccharides. These results fully agree with crystallographic data showing that binding of specific ligands to ConA requires conformational chances of its monosaccharide-binding site.Instituto Oswaldo Cruz, Ministério da Saúde1996-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761996000600021Memórias do Instituto Oswaldo Cruz v.91 n.6 1996reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02761996000600021info:eu-repo/semantics/openAccessRamos,Márcio VianaMoreira,Renato de AzevedoOliveira,José Tadeu AbreuCavada,Benildo SousaRougé,Pierreeng2020-04-25T17:47:36Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:07:14.97Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
title |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
spellingShingle |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins Ramos,Márcio Viana Canavalia maritima carbohydrate-binding specificity Diocleinae Dioclea grandiflora lectins molecular modelling |
title_short |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
title_full |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
title_fullStr |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
title_full_unstemmed |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
title_sort |
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins |
author |
Ramos,Márcio Viana |
author_facet |
Ramos,Márcio Viana Moreira,Renato de Azevedo Oliveira,José Tadeu Abreu Cavada,Benildo Sousa Rougé,Pierre |
author_role |
author |
author2 |
Moreira,Renato de Azevedo Oliveira,José Tadeu Abreu Cavada,Benildo Sousa Rougé,Pierre |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Ramos,Márcio Viana Moreira,Renato de Azevedo Oliveira,José Tadeu Abreu Cavada,Benildo Sousa Rougé,Pierre |
dc.subject.por.fl_str_mv |
Canavalia maritima carbohydrate-binding specificity Diocleinae Dioclea grandiflora lectins molecular modelling |
topic |
Canavalia maritima carbohydrate-binding specificity Diocleinae Dioclea grandiflora lectins molecular modelling |
dc.description.none.fl_txt_mv |
The carbohydrate-binding specificity of lectins from the seeds of Canavalia maritima and Dioclea grandiflora was studied by hapten-inhibition of haemagglutination using various sugars and sugar derivatives as inhibitors, including N-acetylneuraminic acid and N-acetylmuramic acid. Despite some discrepancies, both lectins exhibited a very similar carbohydrate-binding specificity as previously reported for other lectins from Diocleinae (tribe Phaseoleae, sub-tribe Diocleinae). Accordingly, both lectins exhibited almost identical hydropathic profiles and their three-dimensional models built up from the atomic coordinates of ConA looked very similar. However, docking experiments of glucose and mannose in their monosaccharide-binding sites, by comparison with the ConA-mannose complex used as a model, revealed conformational changes in side chains of the amino acid residues involved in the binding of monosaccharides. These results fully agree with crystallographic data showing that binding of specific ligands to ConA requires conformational chances of its monosaccharide-binding site. |
description |
The carbohydrate-binding specificity of lectins from the seeds of Canavalia maritima and Dioclea grandiflora was studied by hapten-inhibition of haemagglutination using various sugars and sugar derivatives as inhibitors, including N-acetylneuraminic acid and N-acetylmuramic acid. Despite some discrepancies, both lectins exhibited a very similar carbohydrate-binding specificity as previously reported for other lectins from Diocleinae (tribe Phaseoleae, sub-tribe Diocleinae). Accordingly, both lectins exhibited almost identical hydropathic profiles and their three-dimensional models built up from the atomic coordinates of ConA looked very similar. However, docking experiments of glucose and mannose in their monosaccharide-binding sites, by comparison with the ConA-mannose complex used as a model, revealed conformational changes in side chains of the amino acid residues involved in the binding of monosaccharides. These results fully agree with crystallographic data showing that binding of specific ligands to ConA requires conformational chances of its monosaccharide-binding site. |
publishDate |
1996 |
dc.date.none.fl_str_mv |
1996-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761996000600021 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761996000600021 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02761996000600021 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
dc.source.none.fl_str_mv |
Memórias do Instituto Oswaldo Cruz v.91 n.6 1996 reponame:Memórias do Instituto Oswaldo Cruz instname:Fundação Oswaldo Cruz instacron:FIOCRUZ |
reponame_str |
Memórias do Instituto Oswaldo Cruz |
collection |
Memórias do Instituto Oswaldo Cruz |
instname_str |
Fundação Oswaldo Cruz |
instacron_str |
FIOCRUZ |
institution |
FIOCRUZ |
repository.name.fl_str_mv |
Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz |
repository.mail.fl_str_mv |
|
_version_ |
1669937667325820928 |