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dc.creatorMurakami, Mário T.
dc.creatorArruda, Emerson Z.
dc.creatorMelo, Paulo A.
dc.creatorMartínez, Ana B.
dc.creatorCalil Elías, Sabriná
dc.creatorTomaz, Marcelo A.
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorArni, Raghuvir K.
dc.date.accessioned2016-12-15T21:21:48Z
dc.date.available2016-12-15T21:21:48Z
dc.date.issued2005-06-15
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S002228360500505Xes_ES
dc.identifier.issn0022-2836
dc.identifier.urihttp://hdl.handle.net/10669/29413
dc.description.abstractSuramin, a synthetic polysulfonated compound, developed initially for the treatment of African trypanosomiasis and onchocerciasis, is currently used for the treatment of several medically relevant disorders. Suramin, heparin, and other polyanions inhibit the myotoxic activity of Lys49 phospholipase A2 analogues both in vitro and in vivo, and are thus of potential importance as therapeutic agents in the treatment of viperid snake bites. Due to its conformational flexibility around the single bonds that link the central phenyl rings to the secondary amide backbone, the symmetrical suramin molecule binds by an induced-fit mechanism complementing the hydrophobic surfaces of the dimer and adopts a novel conformation that lacks C2 symmetry in the dimeric crystal structure of the suramin–Bothrops asper myotoxin II complex. The simultaneous binding of suramin at the surfaces of the two monomers partially restricts access to the nominal active sites and significantly changes the overall charge of the interfacial recognition face of the protein, resulting in the inhibition of myotoxicity.es_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo//FAPESP/Brasiles_ES
dc.description.sponsorshipStructural Molecular Biology Network//SMOLBNet/Brasiles_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior//CAPES/DAAD/Brasiles_ES
dc.description.sponsorshipCentros de Pesquisa, Inovação e Difusão//CEPID/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Rio de Janeiro//FAPERJ/Brasiles_ES
dc.description.sponsorshipPrograma de Apoio a Núcles de Excelência//PRONEX/Brasiles_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Molecular Biology; Volumen 350, Número 3. 2005es_ES
dc.subjectSuramines_ES
dc.subjectHeparines_ES
dc.subjectMyotoxicityes_ES
dc.subjectIinhibitiones_ES
dc.subjectCrystal Structurees_ES
dc.titleInhibition of Myotoxic Activity of Bothrops asper Myotoxin II by the Anti-trypanosomal Drug Suramines_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.jmb.2005.04.072
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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