dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.contributor | Universidade de São Paulo (USP) | |
dc.contributor | Universidade Federal de Rondônia (UNIR) | |
dc.date.accessioned | 2014-05-20T13:49:40Z | |
dc.date.accessioned | 2022-10-05T14:21:34Z | |
dc.date.available | 2014-05-20T13:49:40Z | |
dc.date.available | 2022-10-05T14:21:34Z | |
dc.date.created | 2014-05-20T13:49:40Z | |
dc.date.issued | 2011-08-01 | |
dc.identifier | Acta Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 67, p. 900-902, 2011. | |
dc.identifier | 1744-3091 | |
dc.identifier | http://hdl.handle.net/11449/17707 | |
dc.identifier | 10.1107/S174430911102392X | |
dc.identifier | WOS:000293698400013 | |
dc.identifier | WOS000293698400013.pdf | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/3892347 | |
dc.description.abstract | Phospholipases 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.language | eng | |
dc.publisher | Wiley-Blackwell | |
dc.relation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | |
dc.rights | Acesso aberto | |
dc.source | Web of Science | |
dc.title | Crystallization and preliminary X-ray diffraction studies of BmooPLA(2)-I, a platelet-aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops moojeni venom | |
dc.type | Artigo | |