Crystallization and preliminary X-ray diffraction analysis of a myotoxic Lys49-PLA(2) from Bothrops jararacussu venom complexed with p-bromophenacyl bromide

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T13:49:21Z
dc.date.accessioned2022-10-05T14:20:43Z
dc.date.available2014-05-20T13:49:21Z
dc.date.available2022-10-05T14:20:43Z
dc.date.created2014-05-20T13:49:21Z
dc.date.issued2006-06-01
dc.identifierActa Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 62, p. 600-603, 2006.
dc.identifier1744-3091
dc.identifierhttp://hdl.handle.net/11449/17582
dc.identifier10.1107/S174430910601801X
dc.identifierWOS:000238067600031
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3892249
dc.description.abstractFor the first time, a non-catalytic and myotoxic Lys49-PLA(2) (BthTX-I from Bothrops jararacussu venom) has been crystallized with BPB inhibitor. X-ray diffraction data were collected and electron-density calculations showed that the ligand is bound to the His48 residue. BthTX-I with His48 chemically modified by BPB shows strongly reduced myotoxic and cytotoxic activities. This suggests a biological correlation between the modification of His48, which is associated with catalytic activity of PLA(2)s, and other toxicological activities of Lys49-PLA(2)s.
dc.languageeng
dc.publisherBlackwell Publishing
dc.relationActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystallization and preliminary X-ray diffraction analysis of a myotoxic Lys49-PLA(2) from Bothrops jararacussu venom complexed with p-bromophenacyl bromide
dc.typeArtigo


Este ítem pertenece a la siguiente institución