Native crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritima

Página do item simplificado
dc.contributor.authorGadelha, CAD
dc.contributor.authorMoreno, FBMB
dc.contributor.authorSanti-Gadelha, T.
dc.contributor.authorCajazeiras, J. B.
dc.contributor.authorda Rocha, BAM
dc.contributor.authorAssreuy, AMS
dc.contributor.authorMota, MRL
dc.contributor.authorPinto, N. V.
dc.contributor.authorMeireles, AVP
dc.contributor.authorBorges, J. C.
dc.contributor.authorFreitas, B. T.
dc.contributor.authorCanduri, F.
dc.contributor.authorSouza, E. P.
dc.contributor.authorDelatorre, P.
dc.contributor.authorCriddle, D. N.
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorCavada, B. S.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Ceará (UFC)
dc.contributor.institutionUniv Reg Cariri
dc.contributor.institutionUniv Estadual Ceara
dc.date.accessioned2014-05-20T15:28:30Z
dc.date.available2014-05-20T15:28:30Z
dc.date.issued2005-12-01
dc.description.abstractHere, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of proteins. ConM was crystallized and its structure determined by standard molecular replacement techniques. The amino acid residues, previously suggested incorrectly by manual sequencing, have now been determined as I17, I53, S129, S134, G144, S164, P165, S187, V190, S169, T196, and S202. Analysis of the structure indicated a dimer in the asymmetric unit, two metal binding sites per monomer, and loops involved in the molecular oligomerization. These confer 98% similarity between ConM and other previously described lectins, derived from Canavalia ensiformis and Canavalia brasiliensis. Our functional data indicate that ConM exerts a concentration-dependent relaxant action on isolated aortic rings that probably occurs via an interaction with a specific lectin-binding site on the endothelium, resulting in a release of nitric oxide. (C) 2005 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Estadual Paulista, IBILCE, Dept Fis, São Paulo, Brazil
dc.description.affiliationUniv Fed Ceara, Dept Bioquim & Biol Mol, BioMol Lab, Fortaleza, Ceara, Brazil
dc.description.affiliationUniv Reg Cariri, Dept Biol, Crato, Brazil
dc.description.affiliationUniv Estadual Ceara, Lab Farmacol Canais Ion, Fortaleza, Ceara, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, IBILCE, Dept Fis, São Paulo, Brazil
dc.format.extent185-194
dc.identifierhttp://dx.doi.org/10.1016/j.jsb.2005.07.012
dc.identifier.citationJournal of Structural Biology. San Diego: Academic Press Inc. Elsevier B.V., v. 152, n. 3, p. 185-194, 2005.
dc.identifier.doi10.1016/j.jsb.2005.07.012
dc.identifier.issn1047-8477
dc.identifier.urihttp://hdl.handle.net/11449/38298
dc.identifier.wosWOS:000234443000004
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofJournal of Structural Biology
dc.relation.ispartofjcr3.433
dc.relation.ispartofsjr3,948
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectlegume lectinpt
dc.subjectCanavalia maritimapt
dc.subjectCrystal structurept
dc.subjectnitric oxidept
dc.subjectvascularpt
dc.titleNative crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritimaen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0002-5791-6170[17]
unesp.author.orcid0000-0003-3778-0584[7]
unesp.author.orcid0000-0002-7157-0321[5]
unesp.author.orcid0000-0003-4856-748X[10]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

Arquivos

Licença do Pacote
Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Artigos - Física - IBILCE