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- W2468467265 abstract "Genetic engineering of Cry proteins from Bacillus thuringiensis (BT) has resulted in the synthesis of various novel toxin proteins which exhibits increased insecticidal activity and highly specificity towards different insect pests. The present study focused on computational studies on PirB sequence from Photorhabdus luminescens. The consensus tree generated by PHYLIP for the PirB sequence revealed that this toxin sequence does not share any ancestral relationship with other Cry toxins from Bacillus thuringiensis considered in this study. Molecular modeling of PirB was followed by construction of two fusion proteins: Type I (PirB-Cry2AaII-Cry2AaIII) and Type II (PirB-Cry2AaII-Garlic lectin). Comparison of the 3D model of PirB with X-ray structure of N-terminal domain 1I5P_A revealed both the structures shared similar architecture. Validation of the tertiary structure of PirB by the structural assessment tools such as ProSA, ERRAT and PROCHECK suggested that the predicted structure was of reasonable quality. Docking studies carried out onto the cadherin receptor showed that Type II fusion protein had a greater affinity, suggesting the possibility of using this fusion protein as a potential bio-pesticide." @default.
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- W2468467265 date "2012-01-01" @default.
- W2468467265 modified "2023-09-24" @default.
- W2468467265 title "Molecular Modeling and Docking Studies of PirB Fusion Protein from Photorhabdus Luminescens" @default.
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