Key Amino Acid Residues Involved in Binding Interactions between Bactrocera minax Odorant-Binding Protein 3 (BminOBP3) and Undecanol.

ABSTRACT: Insect odorant-binding proteins (OBPs) are significant in binding and transporting odorants to specific receptors. Our previous study demonstrated that BminOBP3 exhibited a strong affinity with undecanol. However, the binding mechanism between them remains unknown. Here, using homology modeling and molecular docking, we found that the C-terminus (I116-P122), especially the hydrogenbonds formed by the last three amino acid residues (V120, F121, and P122) of the C-terminus, is essential for BminOBP3's ligand binding. Mutant binding assays showed that the mutant T-OBP3 that lacks C-terminus (I116-P122) displayed a significant decrease in affinity to undecanol (K_i = 19.57 ± 0.45) compared with that of the wild-type protein BminOBP3 (K_i = 11.59 ± 0.51). In the mutant 3D2a

SUBMITTER: Yang L 

PROVIDER: S-EPMC10531759 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature