6533b7d8fe1ef96bd126ae2b
RESEARCH PRODUCT
Structural Domains of the Bacillus thuringiensis Vip3Af Protein Unraveled by Tryptic Digestion of Alanine Mutants
Juan FerréYudong Quansubject
Health Toxicology and MutagenesisIn silicoMutantlcsh:MedicineToxicologyCleavage (embryo)03 medical and health sciencesagricultural_sciences_agronomytetrameric proteinsTetramerinsecticidal proteinsmedicineBt toxins030304 developmental biologychemistry.chemical_classificationAlanine0303 health sciences030306 microbiologyChemistrylcsh:RAlanine scanningtrypsin cleavageTrypsinAmino acidBiochemistrydomain mapmedicine.drugdescription
Vip3 proteins are increasingly used in insect control in transgenic crops. To shed light on the structure of these proteins, we used the approach of the trypsin fragmentation of mutants altering the conformation of the Vip3Af protein. From an alanine scanning of Vip3Af, we selected mutants with an altered proteolytic pattern. Based on protease digestion patterns, their effect on oligomer formation, and theoretical cleavage sites, we generated a map of the Vip3Af protein with five domains which match some of the domains proposed independently by two in silico models. Domain I ranges amino acids (aa) 12&ndash
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-06-21 | Toxins |