Author/Authors :
Bhargavi، CH. نويسنده Department of Bioinformatics, Global institute of Biotechnology, Himayat nagar, Hyderabad-29, A.P, INDIA , , Ali، Mohammed Hadi نويسنده Department of Chemistry, Osmania University, Hyderabad, A.P, INDIA. , , Tangeti، Venkata Swamy نويسنده Department of Chemistry, Pondicherry Central University, Pondicherry. , , Konka، Ramesh نويسنده Department of Biotechnology, Akshaya Biological Corporation, Himayat nagar, Hyderabad, A.P, INDIA. , , Daddam، Jayasimha Rayalu نويسنده Department of Biotechnology, DR.Rayalu’s Biotech PVT LTD, Himayat nagar, Hyderabad, A.P, INDIA ,
Abstract :
The epidermal growth factor receptor (EGFR), cell-surface receptor for epidermal growth factor family exists on the cell surface and is activated by binding to epidermal growth factor. Mutations that lead to EGFR over expression have been associated with a number of cancers. In this work we have identified a better inhibitor for mutated EGFR to reduce the Cancer risk. In order to understand the mechanisms of interactions between the drug derivatives and the EGFR, a three-dimensional (3D) model of the EGFR was generated based on the crystal structure of the Template by using Modeller. After BLAST search sequence that showed maximum identity with EGFR was aligned and used as a reference template to build a 3D model for EGFR. The final model obtained was further assessed by ERRAT and Ramachandran plot, which shows that the model is reliable. With this model, a flexible docking study is performed with Gefitinib derivatives. After the docking studies, important determined residues in binding were identified. The hydrogen bonds play an important role for the stability of the complex. These results may be helpful for further experimental investigations.
