Modeling the Trypanosoma cruzi Tc85-11 protein and mapping the laminin-binding site

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dc.contributor.authorMarroquin-Quelopana, M.
dc.contributor.authorOyama, S.
dc.contributor.authorPertinhez, T. A.
dc.contributor.authorSpisni, A.
dc.contributor.authorJuliano, M. A.
dc.contributor.authorJuliano, L.
dc.contributor.authorColli, W.
dc.contributor.authorAlves, MJM
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionLab Nacl Luz Sincrotron
dc.contributor.institutionUniv Parma
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:37:31Z
dc.date.available2016-01-24T12:37:31Z
dc.date.issued2004-12-10
dc.description.abstractTrypanosoma cruzi expresses a set of glycoproteins encoded by the gp85/trans-sialidase gene superfamily. in this report a structure model is proposed for a cloned member of the superfamily, the Tc85-11 protein. the structure consists of an N-terminus beta-propeller and a C-terminus beta-sandwich interconnected by an alpha-helix, the recombinant protein, corresponding to the N-domain (Tc85-N), binds to laminin in a selective manner. Six synthetic 20-mer peptides from the N-domain adhere onto the surface of LLC-MK2 cells and two of these peptides specifically inhibit the Tc85-N/laminin interaction, indicating that they are the laminin-binding sites of the molecule. Thus, Tc85-11 and other related members of the family appear to be good candidates to play an important role in T cruzi infection via a laminin mediated host-parasite interaction. (C) 2004 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniv São Paulo, Inst Quim, BR-05508900 São Paulo, Brazil
dc.description.affiliationLab Nacl Luz Sincrotron, Ctr Biol Mol Estrutural, BR-13084971 Campinas, SP, Brazil
dc.description.affiliationUniv Parma, Dept Expt Med Sec Chem & Struct Biochem, I-43100 Parma, Italy
dc.description.affiliationUniversidade Federal de São Paulo, BR-04023900 São Paulo, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, BR-04023900 São Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.format.extent612-618
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.10.068
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 325, n. 2, p. 612-618, 2004.
dc.identifier.doi10.1016/j.bbrc.2004.10.068
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/28049
dc.identifier.wosWOS:000225279600036
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTrypanosoma cruzien
dc.subjectlamininen
dc.subjectadhesionen
dc.subjectreceptoren
dc.subjectprotein domainsen
dc.subjectsynthetic peptidesen
dc.subjecthomology modelingen
dc.titleModeling the Trypanosoma cruzi Tc85-11 protein and mapping the laminin-binding siteen
dc.typeinfo:eu-repo/semantics/article
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