Preliminary insight into recognizing of mannose toward LSMT Protein: Molecular docking and DFT Study

Abstract

A novel protein like-lectin Light Subunit Mushroom Tyrosinase (LSMT) was discovered inadvertently during elucidation of the button mushroom Agaricus bisporus tyrosinase structure. The present study is focused on investigation of interaction between Mannose and LSMT using molecular docking and Density Functional Theory (DFT). 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 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.