EGFR receptors play an important role in the growth of cancer cells, and these receptors have undergone various types of mutations. At this time, the effect of the L718Q / T790M point mutation on the EGFR receptor is not known, therefore the aim of this study is to predict the EGFR structure with the L718Q / T790M point mutation using in silico homology modeling. The mutant protein was successfully modeled using SWISS-Model expasy webserver and showed good evaluation results after the protein was minimized as indicated by the results of the Ramachandran outlier score of 0%, clashscore 0.98, and MolProbity 1.15. Identification of the active site of the mutant protein shows a conformational change of the active site that causes a steric collision between the inhibitor group and the amino acid side chain of the mutant protein. Keywords: EGFR, mutation, homology modeling, in silico.
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