Structure of a Lys49-Phospholipase A2 homologue isolated from the venom of Bothrops nummifer (jumping viper)
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| Autores: | , , , |
|---|---|
| Formato: | artículo original |
| Fecha de Publicación: | 1999 |
| Descripción: | Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. We have solved the structure of myotoxin-I, a Lys49-PLA2 homologue isolated from the venom of Bothrops nummifer (jumping viper) at 2.4 A resolution using molecular replacement techniques. The final model has been refined to a final R-factor of 18.4% (R-free = 23.2%), and shows excellent geometry. The myotoxin-I from Bothrops nummifer is dimeric in the crystalline state as has been observed for other Lys49-PLA2 homologues. In addition, a continuous electron density in the active site and substrate binding channel could be successfully modeled as a fatty-acid molecule. |
| País: | Kérwá |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Kérwá |
| OAI Identifier: | oai:kerwa.ucr.ac.cr:10669/29448 |
| Acceso en línea: | http://www.sciencedirect.com/science/article/pii/S0041010198001895 https://hdl.handle.net/10669/29448 |
| Palabra clave: | Animals Binding Sites Bothrops Crystallization Dimerization In Vitro Techniques Lysine Molecular Conformation Palmitic Acid Phospholipases A Phospholipases A2 Protein Conformation Sensitivity and Specificity X-Ray Diffraction Snake venom |