dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Federal de Rondônia (UNIR)
dc.date.accessioned2014-05-20T13:49:40Z
dc.date.accessioned2022-10-05T14:21:34Z
dc.date.available2014-05-20T13:49:40Z
dc.date.available2022-10-05T14:21:34Z
dc.date.created2014-05-20T13:49:40Z
dc.date.issued2011-08-01
dc.identifierActa Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 67, p. 900-902, 2011.
dc.identifier1744-3091
dc.identifierhttp://hdl.handle.net/11449/17707
dc.identifier10.1107/S174430911102392X
dc.identifierWOS:000293698400013
dc.identifierWOS000293698400013.pdf
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3892347
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.
dc.languageeng
dc.publisherWiley-Blackwell
dc.relationActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rightsAcesso aberto
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 venom
dc.typeArtigo


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