Structure-function relationship for the highly toxic crotoxin from Crotalus durissus terrificus

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Autor(es): dc.contributorUniversidade de Sáo Paulo-
Autor(es): dc.contributorEuropean Molecular Biology Laboratory-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFaculdade de Medicina de Ribeiráo Preto-
Autor(es): dc.creatorMascarenhas, Yvonne P.-
Autor(es): dc.creatorStouten, Pieter F.W.-
Autor(es): dc.creatorBeltran, José R.-
Autor(es): dc.creatorLaure, Carlos J.-
Autor(es): dc.creatorVriend, Gerrit-
Data de aceite: dc.date.accessioned2025-08-21T22:25:19Z-
Data de disponibilização: dc.date.available2025-08-21T22:25:19Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued1992-07-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1007/BF00196764-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/223942-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/223942-
Descrição: dc.descriptionThe three-dimensional structure of the highly toxic crotoxin from Crotalus durissus terrificus was modelled based on sequence analysis and the refined structure of calcium-free phospholipase of Crotalus atrox venom. Small-angle x-ray scattering experiments were performed on aqueous solutions of crotoxin. The radial distribution function derived from these scattering experiments and the one calculated from the model structure are in good agreement. Crotoxin consists of a basic and an acidic subunit. The model strongly suggests that the overall folding motif of phospholipases has been preserved in both subunits. The basic domain has an intact active site. The residues that are expected to contact the lipid tails of the phospholipid are different from other phospholipases, but they are all hydrophobic. The acidic domain consists of three independent chains interconnected by disulfide bonds. Compared to other phospholipases the active site for the greater part has been preserved in this domain, but it is not very well shielded from solvent. Most residues normally in contact with the lipid tails of the phospholipid are missing, which might explain the acidic subunit's lack of phospholipase activity. A homology between the third chain of the acidic domain and neurophysins suggests that the acidic domain may act as a chaperone for the basic domain. © 1992 Springer-Verlag.-
Descrição: dc.descriptionInstituto de Física e Química de Sáo Carlos Universidade de Sáo Paulo, Sáo Carlos-SP, Caixa Postal 369-13560-
Descrição: dc.descriptionProtein Design Group European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, W-6900-
Descrição: dc.descriptionLetras e Ciências Exatas, UNESP Departamento de Fisica Instituto de Biociências, Sáo José de Rio Preto-SP, Caixa Postal 136-15055-
Descrição: dc.descriptionDepartamento de Bioquimica Faculdade de Medicina de Ribeiráo Preto, Ribeiráo Preto, SP-14100-
Descrição: dc.descriptionLetras e Ciências Exatas, UNESP Departamento de Fisica Instituto de Biociências, Sáo José de Rio Preto-SP, Caixa Postal 136-15055-
Formato: dc.format199-205-
Idioma: dc.languageen-
Relação: dc.relationEuropean Biophysics Journal-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectCrotoxin-
Palavras-chave: dc.subjectModelling by homology-
Palavras-chave: dc.subjectStructure-function relationship-
Palavras-chave: dc.subjectX-ray scattering-
Título: dc.titleStructure-function relationship for the highly toxic crotoxin from Crotalus durissus terrificus-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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