Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: New insights into the understanding of the structure-biological activity relationship in legume lectins

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBezerra, Gustavo Arruda
dc.creatorOliveira, Taiana Maia
dc.creatorMoreno, Frederico Bruno Mendes Batista
dc.creatorDe Souza, Emmanuel Prata
dc.creatorDa Rocha, Bruno Anderson Matias
dc.creatorBenevides, Raquel Guimaraes
dc.creatorDelatorre, Plinio
dc.creatorDe Azevedo, Walter Filgueira
dc.creatorCavada, Benildo Sousa
dc.date2014-05-20T15:22:55Z
dc.date2016-10-25T17:56:44Z
dc.date2014-05-20T15:22:55Z
dc.date2016-10-25T17:56:44Z
dc.date2007-11-01
dc.date.accessioned2017-04-05T23:39:14Z
dc.date.available2017-04-05T23:39:14Z
dc.identifierJournal of Structural Biology. San Diego: Academic Press Inc. Elsevier B.V., v. 160, n. 2, p. 168-176, 2007.
dc.identifier1047-8477
dc.identifierhttp://hdl.handle.net/11449/33809
dc.identifierhttp://acervodigital.unesp.br/handle/11449/33809
dc.identifier10.1016/j.jsb.2007.07.012
dc.identifierWOS:000250456300006
dc.identifierhttp://dx.doi.org/10.1016/j.jsb.2007.07.012
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/877847
dc.descriptionPlant lectins, especially those purified from species of the Legummosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/ efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/ CGL:Man(alpha 1-2)Man(alpha 1-0)Me, ConM/CGL:Man(alpha 1-O)Man(alpha 1-O)Me and ConM/CGL:Man(alpha 1-4)Man(alpha 1-O)Me, which crystallized in different conditions and space group from the native proteins.The structures were solved by molecular replacement, presenting satisfactory values for R-factor and R-factor. Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe. (C) 2007 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationJournal of Structural Biology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectlegume lectin
dc.subjectdimannoside
dc.subjectCanavalia maritima lectin
dc.subjectCanavalia gladiata lectin
dc.titleStructural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: New insights into the understanding of the structure-biological activity relationship in legume lectins
dc.typeOtro


Este ítem pertenece a la siguiente institución