Use este identificador para citar ou linkar para este item: http://repositorio.ufc.br/handle/riufc/64280
Tipo: Artigo de Periódico
Título: Cloning of cDNA sequences encoding cowpea (Vigna unguiculata) vicilins: Computational simulations suggest a binding mode of cowpea vicilins to chitin oligomers
Autor(es): Rocha, Antônio J.
Sousa, Bruno L.
Girão, Matheus S.
Barroso-Neto, Ito L.
Júnior, José E. Monteiro
Oliveira, José Tadeu Abreu de
Nagano, Celso S.
Carneiro, Rômulo F.
Monteiro-Moreira, Ana C. O.
Rocha, Bruno A. M.
Freire, Valder N.
Grangeiro, Thalles B.
Palavras-chave: Callosobruchus maculatus;Chitin-binding proteins;Seed storage proteins
Data do documento: 2018
Instituição/Editor/Publicador: International Journal of Biological Macromolecules
Citação: ROCHA, Antônio J. et al. Cloning of cDNA sequences encoding cowpea (Vigna unguiculata) vicilins: Computational simulations suggest a binding mode of cowpea vicilins to chitin oligomers. International Journal of Biological Macromolecules, [s. l.], v. 117, p. 565-573, 2018.
Abstract: Vicilins are 7S globulins which constitute the major seed storage proteins in leguminous species. Variant vicilins showing differential binding affinities for chitin have been implicated in the resistance and susceptibility of cowpea to the bruchid Callosobruchus maculatus. These proteins are members of the cupin superfamily, which includes a wide variety of enzymes and non-catalytic seed storage proteins. The cupin fold does not share similarity with any known chitin-biding domain. Therefore, it is poorly understood how these storage proteins bind to chitin. In this work, partial cDNA sequences encoding β-vignin, the major component of cowpea vicilins, were obtained from developing seeds. Three-dimensional molecular models of β-vignin showed the characteristic cupin fold and computational simulations revealed that each vicilin trimer contained 3 chitin-binding sites. Interaction models showed that chito-oligosaccharides bound to β-vignin were stabilized mainly by hydrogen bonds, a common structural feature of typical carbohydrate-binding proteins. Furthermore, many of the residues involved in the chitin-binding sites of β-vignin are conserved in other 7S globulins. These results support previous experimental evidences on the ability of vicilin-like proteins from cowpea and other leguminous species to bind in vitro to chitin as well as in vivo to chitinous structures of larval C. maculatus midgut.
URI: http://www.repositorio.ufc.br/handle/riufc/64280
Tipo de Acesso: Acesso Aberto
Aparece nas coleções:DBIO - Artigos publicados em revista científica

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