Download MendeleySuccessful refolding and NMR structure of rMagi3: A disulfide-rich insecticidal spider toxin.
Titaux-Delgado, G., Carrillo, E., Mendoza, A., Mayorga-Flores, M., Escobedo-Gonzalez, F.C., Cano-Sanchez, P., Lopez-Vera, E., Corzo, G., Del Rio-Portilla, F.(2018) Protein Sci 27: 692-701
- PubMed: 29247580
- DOI: https://doi.org/10.1002/pro.3363
- Primary Citation of Related Structures:
6AX2 - PubMed Abstract:
The need for molecules with high specificity against noxious insects leads the search towards spider venoms that have evolved highly selective toxins for insect preys. In this respect, spiders as a highly diversified group of almost exclusive insect predators appear to possess infinite potential for the discovery of novel insect-selective toxins. In 2003, a group of toxins was isolated from the spider Macrothele gigas and the amino acid sequence was reported. We obtained, by molecular biology techniques in a heterologous system, one of these toxins. Purification process was optimized by chromatographic methods to determine the three-dimensional structure by nuclear magnetic resonance in solution, and, finally, their biological activity was tested. rMagi3 resulted to be a specific insect toxin with no effect on mice.
Organizational Affiliation:
Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, CU, Ciudad de México, 04510, México.
