Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth

Detalhes bibliográficos
Autor(a) principal: Alysson Chaves Almeida
Data de Publicação: 2016
Tipo de documento: Tese
Idioma: por
Título da fonte: Biblioteca Digital de Teses e Dissertações da UFC
Texto Completo: http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=17033
Resumo: A glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from the Dalbergieae tribe. CTL was isolated by mannose-Sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids and one N-glycosylation site, possessing high similarity with the lectin Platypodium elegans (PELa) and Pterocarpus angolensis (PAL) derived from the same tribe. Two crystal structures of CTL, with monoclinic and tetragonal forms, both complexed with methyl dimanosÃdeo has been solved at 2.25 and 1.9 Ã, respectively, with high similarity. The lectin adopts a typical canonical dimeric organization of legume lectins. The carbohydrate recognition domain (CRD), metal binding site, and glycosylation site have been characterized and the structural basis for interaction with carbohydrate been elucidated. CTL showed acute inflammatory effect in a paw edema model. The protein structure was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, revealing a higher affinity for trimannosides and their interactions were compared with similar lectins, which have the same binding specificity. This is the first report of a crystal structure of a native mannose lectin / specific glucose Dalbergieae tribe with pro-inflammatory activity
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spelling info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/doctoralThesisStructural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. BenthCaracterizaÃÃo estrutural e biolÃgica de uma lectina de sementes de centrolobium tomentosum guill. ex benth2016-02-18Benildo Sousa Cavada24242349068http://lattes.cnpq.br/5029704662813380 JoÃo Batista Cajazeiras478 389 303 91http://lattes.cnpq.br/1947326193452969 Francisco Nascimento Pereira JÃnior01363350390http://lattes.cnpq.br/0009366744574438Kyria Santiago do Nascimento08671084795http://lattes.cnpq.br/4999713109630711Alana de Freitas Pires92567533320http://lattes.cnpq.br/097964763963233500951629336 http://lattes.cnpq.br/5130160173904989Alysson Chaves AlmeidaUniversidade Federal do CearÃPrograma de PÃs-GraduaÃÃo em BioquÃmicaUFCBRLectina Centrolobium tomentosumEstrutura primÃriaEstrutura cristalogrÃficaAtividade prÃ-inflamatÃria Docking molecularLectin Centrolobium tomentosum Primary structure Crystal structure Proinflammatory activity Molecular dockingBIOQUIMICAA glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from the Dalbergieae tribe. CTL was isolated by mannose-Sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids and one N-glycosylation site, possessing high similarity with the lectin Platypodium elegans (PELa) and Pterocarpus angolensis (PAL) derived from the same tribe. Two crystal structures of CTL, with monoclinic and tetragonal forms, both complexed with methyl dimanosÃdeo has been solved at 2.25 and 1.9 Ã, respectively, with high similarity. The lectin adopts a typical canonical dimeric organization of legume lectins. The carbohydrate recognition domain (CRD), metal binding site, and glycosylation site have been characterized and the structural basis for interaction with carbohydrate been elucidated. CTL showed acute inflammatory effect in a paw edema model. The protein structure was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, revealing a higher affinity for trimannosides and their interactions were compared with similar lectins, which have the same binding specificity. This is the first report of a crystal structure of a native mannose lectin / specific glucose Dalbergieae tribe with pro-inflammatory activityUma lectina glicosilada (CTL) com especificidade a manose e glucose foi detectada e purificada a partir de sementes de Centrolobium Tomentosum, uma leguminosa pertencente à tribo Dalbergieae. CTL foi isolada por cromatografia de afinidade de Sepharose-Manose. A estrutura primÃria foi determinada por espectrometria de massas e consiste em 245 aminoÃcidos e um sitio de ÂNÂ-glicosilaÃÃo, demonstrando similaridade com a lectina de Platypodium elegans (PELa), Pterocarpus angolensis (PAL), dentre outras, oriundas da mesma tribo. Duas estruturas cristalinas de CTL, de formas monoclÃnica e tetragonal, ambas complexadas com metil-dimanosÃdeo, foram resolvidas a 2,25 e 1,9 Ã, respectivamente, apresentando alta similaridade entre si. A lectina mostrou adotar uma organizaÃÃo dimÃrica canÃnica tÃpica de lectinas de leguminosas. O domÃnio de reconhecimento de carboidratos (CRD), local de ligaÃÃo do metal e local de glicosilaÃÃo foram caracterizados e a base estrutural para a interaÃÃo com carboidratos foi elucidado. CTL mostrou efeito inflamatÃrio agudo em um modelo de edema de pata. A estrutura da proteÃna foi submetida a uma anÃlise de interaÃÃes com dimanosÃdeos e trimanosÃdeos por Docking Molecular, revelando sua maior afinidade por trimanosÃdeos e suas interaÃÃes foram comparadas com lectinas similares que possuam a mesma especificidade de ligaÃÃo. Esse à o primeiro relato de estrutura cristalina de uma lectina nativa manose/glucose especÃfica da tribo Dalbergieae com atividade prÃ-inflamatÃriaCoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superiorhttp://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=17033application/pdfinfo:eu-repo/semantics/openAccessporreponame:Biblioteca Digital de Teses e Dissertações da UFCinstname:Universidade Federal do Cearáinstacron:UFC2019-01-21T11:30:25Zmail@mail.com -
dc.title.en.fl_str_mv Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
dc.title.alternative.pt.fl_str_mv CaracterizaÃÃo estrutural e biolÃgica de uma lectina de sementes de centrolobium tomentosum guill. ex benth
title Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
spellingShingle Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
Alysson Chaves Almeida
Lectina
Centrolobium tomentosum
Estrutura primÃria
Estrutura cristalogrÃfica
Atividade prÃ-inflamatÃria
Docking molecular
Lectin
Centrolobium tomentosum
Primary structure
Crystal structure
Proinflammatory activity
Molecular docking
BIOQUIMICA
title_short Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
title_full Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
title_fullStr Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
title_full_unstemmed Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
title_sort Structural and Biological Characterization of a Seed Lectin from Centrolobium tomentosum Guill ex. Benth
author Alysson Chaves Almeida
author_facet Alysson Chaves Almeida
author_role author
dc.contributor.advisor1.fl_str_mv Benildo Sousa Cavada
dc.contributor.advisor1ID.fl_str_mv 24242349068
dc.contributor.advisor1Lattes.fl_str_mv http://lattes.cnpq.br/5029704662813380
dc.contributor.referee1.fl_str_mv JoÃo Batista Cajazeiras
dc.contributor.referee1ID.fl_str_mv 478 389 303 91
dc.contributor.referee1Lattes.fl_str_mv http://lattes.cnpq.br/1947326193452969
dc.contributor.referee2.fl_str_mv Francisco Nascimento Pereira JÃnior
dc.contributor.referee2ID.fl_str_mv 01363350390
dc.contributor.referee2Lattes.fl_str_mv http://lattes.cnpq.br/0009366744574438
dc.contributor.referee3.fl_str_mv Kyria Santiago do Nascimento
dc.contributor.referee3ID.fl_str_mv 08671084795
dc.contributor.referee3Lattes.fl_str_mv http://lattes.cnpq.br/4999713109630711
dc.contributor.referee4.fl_str_mv Alana de Freitas Pires
dc.contributor.referee4ID.fl_str_mv 92567533320
dc.contributor.referee4Lattes.fl_str_mv http://lattes.cnpq.br/0979647639632335
dc.contributor.authorID.fl_str_mv 00951629336
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/5130160173904989
dc.contributor.author.fl_str_mv Alysson Chaves Almeida
contributor_str_mv Benildo Sousa Cavada
JoÃo Batista Cajazeiras
Francisco Nascimento Pereira JÃnior
Kyria Santiago do Nascimento
Alana de Freitas Pires
dc.subject.por.fl_str_mv Lectina
Centrolobium tomentosum
Estrutura primÃria
Estrutura cristalogrÃfica
Atividade prÃ-inflamatÃria
Docking molecular
topic Lectina
Centrolobium tomentosum
Estrutura primÃria
Estrutura cristalogrÃfica
Atividade prÃ-inflamatÃria
Docking molecular
Lectin
Centrolobium tomentosum
Primary structure
Crystal structure
Proinflammatory activity
Molecular docking
BIOQUIMICA
dc.subject.eng.fl_str_mv Lectin
Centrolobium tomentosum
Primary structure
Crystal structure
Proinflammatory activity
Molecular docking
dc.subject.cnpq.fl_str_mv BIOQUIMICA
dc.description.sponsorship.fl_txt_mv CoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superior
dc.description.abstract.por.fl_txt_mv A glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from the Dalbergieae tribe. CTL was isolated by mannose-Sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids and one N-glycosylation site, possessing high similarity with the lectin Platypodium elegans (PELa) and Pterocarpus angolensis (PAL) derived from the same tribe. Two crystal structures of CTL, with monoclinic and tetragonal forms, both complexed with methyl dimanosÃdeo has been solved at 2.25 and 1.9 Ã, respectively, with high similarity. The lectin adopts a typical canonical dimeric organization of legume lectins. The carbohydrate recognition domain (CRD), metal binding site, and glycosylation site have been characterized and the structural basis for interaction with carbohydrate been elucidated. CTL showed acute inflammatory effect in a paw edema model. The protein structure was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, revealing a higher affinity for trimannosides and their interactions were compared with similar lectins, which have the same binding specificity. This is the first report of a crystal structure of a native mannose lectin / specific glucose Dalbergieae tribe with pro-inflammatory activity
Uma lectina glicosilada (CTL) com especificidade a manose e glucose foi detectada e purificada a partir de sementes de Centrolobium Tomentosum, uma leguminosa pertencente à tribo Dalbergieae. CTL foi isolada por cromatografia de afinidade de Sepharose-Manose. A estrutura primÃria foi determinada por espectrometria de massas e consiste em 245 aminoÃcidos e um sitio de ÂNÂ-glicosilaÃÃo, demonstrando similaridade com a lectina de Platypodium elegans (PELa), Pterocarpus angolensis (PAL), dentre outras, oriundas da mesma tribo. Duas estruturas cristalinas de CTL, de formas monoclÃnica e tetragonal, ambas complexadas com metil-dimanosÃdeo, foram resolvidas a 2,25 e 1,9 Ã, respectivamente, apresentando alta similaridade entre si. A lectina mostrou adotar uma organizaÃÃo dimÃrica canÃnica tÃpica de lectinas de leguminosas. O domÃnio de reconhecimento de carboidratos (CRD), local de ligaÃÃo do metal e local de glicosilaÃÃo foram caracterizados e a base estrutural para a interaÃÃo com carboidratos foi elucidado. CTL mostrou efeito inflamatÃrio agudo em um modelo de edema de pata. A estrutura da proteÃna foi submetida a uma anÃlise de interaÃÃes com dimanosÃdeos e trimanosÃdeos por Docking Molecular, revelando sua maior afinidade por trimanosÃdeos e suas interaÃÃes foram comparadas com lectinas similares que possuam a mesma especificidade de ligaÃÃo. Esse à o primeiro relato de estrutura cristalina de uma lectina nativa manose/glucose especÃfica da tribo Dalbergieae com atividade prÃ-inflamatÃria
description A glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from the Dalbergieae tribe. CTL was isolated by mannose-Sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids and one N-glycosylation site, possessing high similarity with the lectin Platypodium elegans (PELa) and Pterocarpus angolensis (PAL) derived from the same tribe. Two crystal structures of CTL, with monoclinic and tetragonal forms, both complexed with methyl dimanosÃdeo has been solved at 2.25 and 1.9 Ã, respectively, with high similarity. The lectin adopts a typical canonical dimeric organization of legume lectins. The carbohydrate recognition domain (CRD), metal binding site, and glycosylation site have been characterized and the structural basis for interaction with carbohydrate been elucidated. CTL showed acute inflammatory effect in a paw edema model. The protein structure was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, revealing a higher affinity for trimannosides and their interactions were compared with similar lectins, which have the same binding specificity. This is the first report of a crystal structure of a native mannose lectin / specific glucose Dalbergieae tribe with pro-inflammatory activity
publishDate 2016
dc.date.issued.fl_str_mv 2016-02-18
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/doctoralThesis
status_str publishedVersion
format doctoralThesis
dc.identifier.uri.fl_str_mv http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=17033
url http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=17033
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Federal do CearÃ
dc.publisher.program.fl_str_mv Programa de PÃs-GraduaÃÃo em BioquÃmica
dc.publisher.initials.fl_str_mv UFC
dc.publisher.country.fl_str_mv BR
publisher.none.fl_str_mv Universidade Federal do CearÃ
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UFC
instname:Universidade Federal do Ceará
instacron:UFC
reponame_str Biblioteca Digital de Teses e Dissertações da UFC
collection Biblioteca Digital de Teses e Dissertações da UFC
instname_str Universidade Federal do Ceará
instacron_str UFC
institution UFC
repository.name.fl_str_mv -
repository.mail.fl_str_mv mail@mail.com
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