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DC Field | Value | Language |
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dc.contributor.author | Fortes-Dias, Consuelo Latorre | - |
dc.contributor.author | Marques dos Santos, Roberta Marcia | - |
dc.contributor.author | Magro, Angelo Jose | - |
dc.contributor.author | de Mattos Fontes, Marcos Roberto | - |
dc.contributor.author | Chavez-Olortegui, Carlos | - |
dc.contributor.author | Granier, Claude | - |
dc.date.accessioned | 2014-05-20T13:49:31Z | - |
dc.date.accessioned | 2016-10-25T17:01:58Z | - |
dc.date.available | 2014-05-20T13:49:31Z | - |
dc.date.available | 2016-10-25T17:01:58Z | - |
dc.date.issued | 2009-11-01 | - |
dc.identifier | http://dx.doi.org/10.1016/j.biochi.2009.08.006 | - |
dc.identifier.citation | Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 91, n. 11-12, p. 1482-1492, 2009. | - |
dc.identifier.issn | 0300-9084 | - |
dc.identifier.uri | http://hdl.handle.net/11449/17654 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/17654 | - |
dc.description.abstract | Crotoxin (CA.CB) is a beta-neurotoxin from Crotalus durissus terrificus snake venom that is responsible for main envenomation effects upon biting by this snake. It is a heterodimer of an acidic protein (CA) devoid of any biological activity per se and a basic, enzymatically active, PLA(2) counterpart (CB). Both lethal and enzymatic activities of crotoxin have been shown to be inhibited by CNF, a protein from the blood of C. d. terrificus snakes. CNF replaces CA in the CA-CB complex, forming a stable, non-toxic complex CNF.CB. The molecular sites involved in the tight interfacial protein-protein interactions in these PLA(2)-based complexes have not been clearly determined. To help address this question, we used the peptide arrays approach to map possible interfacial interaction sites in CA.CB and CNF.CB. Amino acid stretches putatively involved in these interactions were firstly identified in the primary structure of CB. Further analysis of the interfacial availability of these stretches in the presumed biologically active structure of CB, suggested two interaction main sites, located at the amino-terminus and beta-wing regions. Peptide segments at the carboxyl-terminus of CB were also suggested to play a secondary role in the binding of both CA and CNF. (C) 2009 Elsevier Masson SAS. All rights reserved. | en |
dc.description.sponsorship | Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG) | - |
dc.description.sponsorship | Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) | - |
dc.format.extent | 1482-1492 | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier France-editions Scientifiques Medicales Elsevier | - |
dc.source | Web of Science | - |
dc.subject | Phospholipase A(2) inhibitor | en |
dc.subject | Crotoxin | en |
dc.subject | Phospholipase A(2) | en |
dc.subject | SPOT synthesis | en |
dc.subject | Crotalus durissus | en |
dc.title | Identification of continuous interaction sites in PLA(2)-based protein complexes by peptide arrays | en |
dc.type | outro | - |
dc.contributor.institution | FUNED | - |
dc.contributor.institution | Universidade Federal de Minas Gerais (UFMG) | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.contributor.institution | Fac Pharm Montpellier | - |
dc.description.affiliation | FUNED, Ctr Res & Dev, BR-30510010 Belo Horizonte, MG, Brazil | - |
dc.description.affiliation | Universidade Federal de Minas Gerais (UFMG), Dept Biochem & Immunol, BR-31270901 Belo Horizonte, MG, Brazil | - |
dc.description.affiliation | UNESP, Inst Biociencias, Dept Phys & Biophys, Botucatu, SP, Brazil | - |
dc.description.affiliation | Fac Pharm Montpellier, Ctr Pharmacol & Hlth Biotechnol, CNRS, UMR 5160, F-34093 Montpellier 5, France | - |
dc.description.affiliationUnesp | UNESP, Inst Biociencias, Dept Phys & Biophys, Botucatu, SP, Brazil | - |
dc.identifier.doi | 10.1016/j.biochi.2009.08.006 | - |
dc.identifier.wos | WOS:000272781500017 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | Biochimie | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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