TAF PUBLISHING

The present study focuses on investigating the interaction between Mannose and LSMT using molecular docking and Density Functional Theory (DFT). A novel protein like-lectin Light Subunit Mushroom Tyrosinase (LSMT) was discovered inadvertently during elucidation of the button mushroom Agaricus bisporus tyrosinase structure. The molecular docking result revealed three possible positions, of which the first resembles the sugar-binding region in the structures of its homolog (HA-33 or CNL), and the second is located in the interface region to the tyrosinase subunit. Another position is a new finding region that includes interaction with five amino acid residues. The molecule complex was modeled by truncation of five selected residues, then the atom of peptide chain freezed. In the final study, the interaction energy was analyzed using DFT showed that Threonine 91 (Thr91) has the highest role of interaction between ligand and protein. Study at this fundamental level is important because it will be used as a benchmark of interaction characteristics between LSMT and Mannose. Thus, the calculation result can be a reference in the development of LSMT application as a drug carrier protein.