| The effects of Tyrosine mutation on PTEN by PyMol |
| Paper ID : 1248-IGA |
| Authors |
|
Parand TorabiParizi *1, Bita Hosseini2 1Parand TorabiParizi, Department of Biology, Faculty of Basic Sciences, Damghan Branch, Islamic Azad University, Damghan, Iran. 2Bita Hosseini, School of Health and life Sciences, Aston University, Birmingham, UK |
| Abstract |
| PTEN is a well-known tumor suppressor protein that plays a crucial role in regulating cell proliferation, survival, and migration through its lipid phosphatase activity. Tyrosine residues within the PTEN structure are essential for keeping the protein stable and functional. In this study, we used PyMOL, a molecular visualization and modeling tool, to investigate how mutations at certain tyrosine sites affect the 3D structure of PTEN. We introduced point mutations and closely examined how these changes influenced areas near the active site and regions that interact with the cell membrane. Our results showed that certain mutations caused noticeable changes in PTEN’s shape, which could interfere with its enzymatic activity and reduce its interaction with the cell membrane. These structural changes might weaken its tumor-suppressing function and contribute to cancer-related processes. This study highlights the usefulness of computer-based structural analysis in understanding how specific mutations affect protein behavior and their possible role in disease development. |
| Keywords |
| PTEN, Tumor suppressor, Tyrosine mutation, Protein structure, PyMOL |
| Status: Accepted |
