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dc.creatorAngulo Ugalde, Yamileth
dc.creatorOlamendi Portugal, Timoteo
dc.creatorAlape Girón, Alberto
dc.creatorPossani, Lourival D.
dc.creatorLomonte, Bruno
dc.date.accessioned2017-12-20T14:34:37Z
dc.date.available2017-12-20T14:34:37Z
dc.date.issued2002
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S1357272502000602es_ES
dc.identifier.issn1357-2725
dc.identifier.urihttp://hdl.handle.net/10669/73710
dc.description.abstractIn order to analyze its structure–function relationships, the complete amino acid sequence of myotoxin II from Atropoides (Bothrops) nummifer from Costa Rica was determined. This toxin is a Lys49-type phospholipase A2 (PLA2) homologue, devoid of catalytic activity, structurally belonging to class IIA. In addition to the Asp49 → Lys change in the (inactive) catalytic center, substitutions in the calcium-binding loop suggest that its lack of enzymatic activity is due to the loss of ability to bind Ca2+. The toxin occurs as a homodimer of basic subunits of 121 residues. Its sequence has highest similarity to Lys49 PLA2s from Cerrophidion, Trimeresurus, Bothrops and Agkistrodon species, which form a subfamily of proteins that diverged early from Asp49 PLA2s present in the same species, as shown by phylogenetic analysis. The tertiary structure of the toxin was modeled, based on the coordinates of Cerrophidion godmani myotoxin II. Its exposed C-terminal region 115–129 shows several differences in comparison to the homologous sequences of other Lys49 PLA2s, i.e. from Agkistrodon p. piscivorus and Bothrops asper. Region 115–129 of the latter two proteins has been implicated in myotoxic activity, on the basis of the direct membrane-damaging of their corresponding synthetic peptides. However, peptide 115–129 of A. nummifer myotoxin II did not exert toxicity upon cultured skeletal muscle cells or mature muscle in vivo. Differences in several amino acid residues, either critical for toxicity, or influencing the conformation of free peptide 115–129 from A. nummifer myotoxin II, may account for its lack of direct membrane-damaging properties.es_ES
dc.description.sponsorshipInternational Foundation for Science/[F/2766-1]/IFS/Sueciaes_ES
dc.description.sponsorshipSecretarı́a de Relaciones Exteriores de México, Bilateral Scientific Cooperation Program Costa Rica-Mexico/[302CR046]//Méxicoes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[VI-741-99-269]/UCR/Costa Ricaes_ES
dc.description.sponsorshipConsejo Nacional para Investigaciones Cientı́ficas y Tecnológicas/[98-013-FO]/CONICIT/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceInternational Journal of Biochemistry and Cell Biology 34(10), 1268-78 (2002)es_ES
dc.subjectmyotoxines_ES
dc.subjectPhospholipase A2es_ES
dc.subjectAtropoides nummiferes_ES
dc.subjectBothropses_ES
dc.subjectSnake venomes_ES
dc.titleStructural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A2 homologuees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/S1357-2725(02)00060-2
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid12127577


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