02719nas a2200397   4500008004100000024000700041245006900048210006600117260001800183300001200201490000700213520162000220653000901840653002001849653002801869653002101897100002101918700002001939700002301959700001601982700002601998700002402024700001702048700001802065700001902083700002502102700001702127700002602144700001602170700001802186700001602204700001702220700002402237700002002261856004002281       2022                        eng d  a2100aAn In Silico Study to Explore the Role of EGFR in Ovarian Cancer0 aIn Silico Study to Explore the Role of EGFR in Ovarian Cancer  cDecember 2022  a817-8210 v143 a<p class="rtejustify">EGFR is a tyrosine kinase receptor that has a role in the tumorigenesis of many types of solid tumors. Aberrantly phosphorylated or overexpressed EGFR is associated with cellular proliferation, prevention of apoptosis, activation of invasion and metastasis, and stimulation of tumor-induced neovascularization. EGFR’s hyperactivity has been observed in ovarian cancer. Although conventional chemotherapy and surgery for advanced ovarian cancer have improved over the years, still there is a critical need for the development of molecular targeted therapies. The major challenge for this approach is the complete understanding of the protein structure of this mega receptor. In this study, we explored this receptor using <em>in silico</em> tools. The protein structure of the EGFR kinase domain (PDB ID: 1M17) and co-crystal containing EGFR and PTP1B kinase domain fragment (PDB ID: 3I7Z) were obtained from the RCSB Protein Data Bank. We performed protein-protein docking using BioLuminate. It was found in this study that the DADEYL segment of EGFR (position 988-993) which includes autophosphorylated tyrosine at position 992, is the segment that is responsible for the overexpression of this receptor in ovarian cancer. There are currently two main classes of clinically-approved drugs which downregulate EGFR activity; tyrosine kinase inhibitors (TKIs) and monoclonal antibodies (Mabs). However, treatment with both type of therapies has been met with shortcomings. Therefore, there is a need for further studies to explore the suitable ligands that can downregulate its activity.</p>
10aEGFR10aIn silico study10aProtein-protein docking10aTyrosine kinases1 aJakhmola, Vikash1 aParashar, Tarun1 aGhildiyal, Pallavi1 aAnsori, ANM1 aSharma, Rajeev, Kumar1 aRao, N., G. Raghave1 aKalra, Kapil1 aSingh, Nishan1 aNainwal, Nidhi1 aSingh, Rajeev, Kumar1 aSingh, M., P1 aKimothi, Vishwadeepak1 aBhatt, Alok1 aDimri, Ashish1 aKumar, Ravi1 aSemwal, Amit1 aAini, Nur, Sofiatul1 aRebezov, Maksim  uhttps://www.phcogj.com/article/1914