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dc.contributor.authorShimabuku, Patricia S. [UNESP]
dc.contributor.authorFernandes, Carlos A. H. [UNESP]
dc.contributor.authorMagro, Angelo J. [UNESP]
dc.contributor.authorCosta, Tassia R.
dc.contributor.authorSoares, Andreimar M.
dc.contributor.authorFontes, Marcos R. M. [UNESP]
dc.date.accessioned2014-05-20T13:49:39Z
dc.date.available2014-05-20T13:49:39Z
dc.date.issued2011-02-01
dc.identifierhttp://dx.doi.org/10.1107/S1744309110051407
dc.identifier.citationActa Crystallographica Section F-structural Biology and Crystallization Communications. Malden: Wiley-blackwell, v. 67, p. 249-252, 2011.
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/11449/17705
dc.description.abstractPhospholipases A(2) (PLA(2)s) are one of the main components of bothropic venoms; in addition to their phospholipid hydrolysis action, they are involved in a wide spectrum of pharmacological activities, including neurotoxicity, myotoxicity and cardiotoxicity. Caffeic acid is an inhibitor that is present in several plants and is employed for the treatment of ophidian envenomations in the folk medicine of many developing countries; as bothropic snake bites are not efficiently neutralized by conventional serum therapy, it may be useful as an antivenom. In this work, the cocrystallization and preliminary X-ray diffraction analysis of the Lys49-PLA(2) piratoxin I from Bothrops pirajai venom in the presence of the inhibitor caffeic acid (CA) are reported. The crystals diffracted X-rays to 1.65 angstrom resolution and the structure was solved by molecular-replacement techniques. The electron-density map unambiguously indicated the presence of three CA molecules that interact with the C-terminus of the protein. This is the first time a ligand has been observed bound to this region and is in agreement with various experiments previously reported in the literature.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.extent249-252
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 analysis of a Lys49-phospholipase A(2) complexed with caffeic acid, a molecule with inhibitory properties against snake venomsen
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.description.affiliationUniv Estadual Paulista, UNESP, Dept Fis & Biofis, Inst Biociencias, Botucatu, SP, Brazil
dc.description.affiliationUSP, FCFRP, Dept Anal Clin Toxicol & Bromatol, Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, UNESP, Dept Fis & Biofis, Inst Biociencias, Botucatu, SP, Brazil
dc.identifier.doi10.1107/S1744309110051407
dc.identifier.wosWOS:000287030600017
dc.rights.accessRightsAcesso aberto
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
dc.identifier.fileWOS000287030600017.pdf
unesp.author.lattes0059017255172730[3]
unesp.author.orcid0000-0002-4634-6221[6]
unesp.author.orcid0000-0001-6515-6872[2]
unesp.author.orcid0000-0002-4253-6992[3]
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