Modeling and molecular dynamics indicate that snake venom phospholipase B-like enzymes are Ntn-hydrolases

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dc.contributor.authorCoronado, Mônika Aparecida [UNESP]
dc.contributor.authorda Silva Olivier, Danilo [UNESP]
dc.contributor.authorEberle, Raphael Josef [UNESP]
dc.contributor.authordo Amaral, Marcos Serrou
dc.contributor.authorArni, Raghuvir Krishnaswamy [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de Mato Grosso do Sul (UFMS)
dc.date.accessioned2018-12-11T17:22:36Z
dc.date.available2018-12-11T17:22:36Z
dc.date.issued2018-10-01
dc.description.abstractPhospholipase-B-like (SVPLB-like) enzymes are present in relatively small amounts in a number of venoms, however, their biological function and mechanisms of action are un-clear. A three-dimensional model of the SVPLB-like enzyme from Crotalus adamanteus was generated by homology modeling based on the crystal structures of bovine Ntn-hydrolyases and the modeled protein possesses conserved domains characteristic of Ntn-hydrolases. Molecular dynamics simulations indicate that activation by autocatalytic cleavage results in the removal of 25 amino acids which increases accessibility to the active site. SVPLB-like enzymes possess a highly reactive cysteine and are hence amidases that to belong to the N-terminal nucleophile (Ntn) hydrolase family. The Ntn-hydrolases (N-terminal nucleophile) form a superfamily of diverse enzymes that are activated autocatalytically; wherein the N-terminal catalytic nucleophile is implicated in the cleavage of the amide bond.en
dc.description.affiliationMultiuser Center for Biomolecular Innovation Department of Physics Universidade Estadual Paulista UNESP/Ibilce, São Jose do Rio Preto
dc.description.affiliationInstitute of Physics Universidade Federal de Mato Grosso do Sul
dc.description.affiliationCentro Multiusuário de Inovação Biomolecular Departamento de Física Instituto de Biociências Letras e Ciências Exatas (Ibilce) Universidade Estadual Paulista (UNESP), Rua Cristóvão Colombo 2265, São Jose do Rio Preto
dc.description.affiliationUnespMultiuser Center for Biomolecular Innovation Department of Physics Universidade Estadual Paulista UNESP/Ibilce, São Jose do Rio Preto
dc.description.affiliationUnespCentro Multiusuário de Inovação Biomolecular Departamento de Física Instituto de Biociências Letras e Ciências Exatas (Ibilce) Universidade Estadual Paulista (UNESP), Rua Cristóvão Colombo 2265, São Jose do Rio Preto
dc.description.sponsorshipFundação de Apoio ao Desenvolvimento do Ensino, Ciência e Tecnologia do Estado de Mato Grosso do Sul
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFundação de Apoio ao Desenvolvimento do Ensino, Ciência e Tecnologia do Estado de Mato Grosso do Sul: 2009/53989-4
dc.description.sponsorshipIdFAPESP: 2015/13765-0
dc.description.sponsorshipIdFAPESP: 2015/18868-2
dc.description.sponsorshipIdFAPESP: 2016/08104-8
dc.description.sponsorshipIdFAPESP: 2016/12904-0
dc.description.sponsorshipIdCAPES: 23/200.307/2014
dc.description.sponsorshipIdCNPq: 307338/2014-2
dc.description.sponsorshipIdCNPq: 401270/2014-9
dc.description.sponsorshipIdCNPq: 435913/2016-6
dc.format.extent106-113
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2018.08.014
dc.identifier.citationToxicon, v. 153, p. 106-113.
dc.identifier.doi10.1016/j.toxicon.2018.08.014
dc.identifier.file2-s2.0-85052967692.pdf
dc.identifier.issn1879-3150
dc.identifier.issn0041-0101
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.scopus2-s2.0-85052967692
dc.identifier.urihttp://hdl.handle.net/11449/176812
dc.language.isoeng
dc.relation.ispartofToxicon
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectCrotalus adamanteus
dc.subjectMolecular dynamics
dc.subjectMolecular modeling
dc.subjectNtn-hydrolase
dc.subjectSnake venom phospholipase B
dc.titleModeling and molecular dynamics indicate that snake venom phospholipase B-like enzymes are Ntn-hydrolasesen
dc.typeResenha
unesp.author.lattes9162508978945887[5]
unesp.author.orcid0000-0002-6518-6497[1]
unesp.author.orcid0000-0003-1269-3783[2]
unesp.author.orcid0000-0001-8101-6933[4]
unesp.author.orcid0000-0003-2460-1145[5]

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Artigos - Física - IBILCE