| Human Fyn tyrosine kinase, a Src-family enzyme plays a pivotal role in the integrin mediated cell signaling pathway and is known to interact with several molecular signals including FAK and paxillin that accounts for morphogenic transformation leading to cancer. The present study was aimed to design a persuasive inhibitor for Fyn kinase. The crystal structure was optimized and energy minimized applying OPLS2001 force field in Maestro v9.0. The inhibitor binding site residues such as LEU-17, GLY-18, ASN-19, VAL-25, ALA-37, LYS-39, GLU-54, THR-82, GLU-83, TYR-84, MET-85, GLY-88, ALA-134, ASN-135, LEU-137, and ASP-148 were located from the Fyn kinase co-crystal structure with staurosporine. Three published inhibitors (staurosporine, Rosmarinic acid and... |
