Molecular modeling of Bt Cry1Ac (DI-DII)-ASAL (Allium sativum lectin)-fusion protein and its interaction with aminopeptidase N (APN) receptor of Manduca sexta
| Autor: | Dayakar Boddupally, Rambabu Gundla, Ramadevi Sanam, Dashavantha Reddy Vudem, Neha S. Gandhi, Ricardo L. Mancera, Venkateswara Rao Khareedu, Sunita Tajne |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Protein Conformation Recombinant Fusion Proteins Molecular Sequence Data Molecular binding Biology CD13 Antigens Molecular Dynamics Simulation Protein Engineering Hemolysin Proteins Protein structure Bacterial Proteins Lectins Manduca Materials Chemistry Animals Homology modeling Amino Acid Sequence Physical and Theoretical Chemistry Binding site Garlic Peptide sequence Spectroscopy Binding Sites Bacillus thuringiensis Toxins fungi Hydrogen Bonding Protein engineering Computer Graphics and Computer-Aided Design Fusion protein Protein Structure Tertiary Endotoxins Biochemistry Docking (molecular) Insect Proteins |
| Zdroj: | Journal of molecular graphicsmodelling. 33 |
| ISSN: | 1873-4243 |
| Popis: | Genetic engineering of Bacillus thuringiensis (Bt) Cry proteins has resulted in the synthesis of various novel toxin proteins with enhanced insecticidal activity and specificity towards different insect pests. In this study, a fusion protein consisting of the DI–DII domains of Cry1Ac and garlic lectin (ASAL) has been designed in silico by replacing the DIII domain of Cry1Ac with ASAL. The binding interface between the DI–DII domains of Cry1Ac and lectin has been identified using protein–protein docking studies. Free energy of binding calculations and interaction profiles between the Cry1Ac and lectin domains confirmed the stability of fusion protein. A total of 18 hydrogen bonds was observed in the DI–DII–lectin fusion protein compared to 11 hydrogen bonds in the Cry1Ac (DI–DII–DIII) protein. Molecular mechanics/Poisson–Boltzmann (generalized-Born) surface area [MM/PB (GB) SA] methods were used for predicting free energy of interactions of the fusion proteins. Protein–protein docking studies based on the number of hydrogen bonds, hydrophobic interactions, aromatic–aromatic, aromatic–sulphur, cation–pi interactions and binding energy of Cry1Ac/fusion proteins with the aminopeptidase N (APN) of Manduca sexta rationalised the higher binding affinity of the fusion protein with the APN receptor compared to that of the Cry1Ac–APN complex, as predicted by ZDOCK, Rosetta and ClusPro analysis. The molecular binding interface between the fusion protein and the APN receptor is well packed, analogously to that of the Cry1Ac–APN complex. These findings offer scope for the design and development of customized fusion molecules for improved pest management in crop plants. |
| Databáze: | OpenAIRE |
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