Show simple item record

dc.contributor.authorSalvador, Guilherme H. M. [UNESP]
dc.contributor.authorMarchi-Salvador, Daniela P. [UNESP]
dc.contributor.authorSilveira, Lucas B.
dc.contributor.authorSoares, Andreimar M.
dc.contributor.authorFontes, Marcos R. M. [UNESP]
dc.date.accessioned2014-05-20T13:49:40Z
dc.date.available2014-05-20T13:49:40Z
dc.date.issued2011-08-01
dc.identifierhttp://dx.doi.org/10.1107/S174430911102392X
dc.identifier.citationActa Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 67, p. 900-902, 2011.
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/11449/17707
dc.description.abstractPhospholipases A(2) (PLA(2)s) are enzymes that cause the liberation of fatty acids and lysophospholipids by the hydrolysis of membrane phospholipids. In addition to their catalytic action, a wide variety of pharmacological activities have been described for snake-venom PLA(2)s. BmooPLA(2)-I is an acidic, nontoxic and catalytic PLA(2) isolated from Bothrops moojeni snake venom which exhibits an inhibitory effect on platelet aggregation, an immediate decrease in blood pressure, inducing oedema at a low concentration, and an effective bactericidal effect. BmooPLA(2)-I has been crystallized and X-ray diffraction data have been collected to 1.6 angstrom resolution using a synchrotron-radiation source. The crystals belonged to space group C222(1), with unit-cell parameters a = 39.7, b = 53.2, c = 89.2 angstrom. The molecular-replacement solution of BmooPLA(2)-I indicated a monomeric conformation, which is in agreement with nondenaturing electrophoresis and dynamic light-scattering experiments. A comparative study of this enzyme with the acidic PLA(2) from B. jararacussu (BthA-I) and other toxic and nontoxic PLA(2)s may provide important insights into the functional aspects of this class of proteins.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipLaboratório Nacional de Luz Síncrotron (LNLS)
dc.format.extent900-902
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.sourceWeb of Science
dc.titleCrystallization and preliminary X-ray diffraction studies of BmooPLA(2)-I, a platelet-aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops moojeni venomen
dc.typeArtigo
dcterms.licensehttp://journals.iucr.org/services/copyrightpolicy.html
dcterms.rightsHolderWiley-blackwell
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de Rondônia (UNIR)
dc.description.affiliationUNESP Univ Estadual Paulista, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.description.affiliationCNPq, Inst Nacl Ciência & Tecnol Toxinas, Brasilia, DF, Brazil
dc.description.affiliationUniv São Paulo, FCFRP, Dept Anal Clin Toxicol & Bromatol, Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv Fed Rondonia, Fundação Oswaldo Cruz, FIOCRUZ Rondonia, Porto Velho, RO, Brazil
dc.description.affiliationUniv Fed Rondonia, Ctr Estudos Biomol Aplicadas CEBio, Porto Velho, RO, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.identifier.doi10.1107/S174430911102392X
dc.identifier.wosWOS:000293698400013
dc.rights.accessRightsAcesso aberto
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
dc.identifier.fileWOS000293698400013.pdf
unesp.author.orcid0000-0002-4634-6221[5]
Localize o texto completo

Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record