Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani

dc.creatorArni, Raghuvir K.
dc.creatorFontes, Marcos Roberto de Mattos
dc.creatorBarberato, C.
dc.creatorGutiérrez, José María
dc.creatorDíaz Oreiro, Cecilia
dc.creatorWard, Richard John
dc.date.accessioned2017-01-23T16:08:35Z
dc.date.accessioned2022-10-19T23:51:52Z
dc.date.available2017-01-23T16:08:35Z
dc.date.available2022-10-19T23:51:52Z
dc.date.created2017-01-23T16:08:35Z
dc.date.issued1999-06-15
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0003986199912109
dc.identifier0003-9861
dc.identifierhttps://hdl.handle.net/10669/29449
dc.identifier10.1006/abbi.1999.1210
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4525049
dc.description.abstractLys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A resolution by molecular replacement. The final model has been refined to a final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with excellent stereochemistry. godMT-II is also monomeric in the crystalline state, and small-angle X-ray scattering results demonstrate that the protein is monomeric in solution under fisicochemical conditions similar to those used in the crystallographic studies.
dc.languageen_US
dc.sourceArchives of Biochemistry and Biophysics; Volumen 366, Número 2, 1999
dc.subjectLys49-Phospholipase A2
dc.subjectCerrophidion (Bothrops) godmani
dc.subjectMyotoxins
dc.subjectSnake venom
dc.titleCrystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani
dc.typeartículo científico


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