Interaction Analysis of Odorant-Binding Protein 12 from Sirex noctilio and Volatiles from Host Plants and Symbiotic Fungi Based on Molecule Dynamics Simulation

As a quarantine pest of conifer, Sirex noctilio has caused widespread harm around the world. It is expected that molecular mechanism protein–ligand binding can be elucidated to carry out control. Through studies SnocOBP12–ligand hydrophobic and dynamics responsible amino acid residues identification, we got some promising results. SnocOBP12 had general excellent affinity for host plant volatiles, may key protein S. find plants. Among many odor molecules are bound SnocOBP12, (?)-?-cedrene (E)-?-farnesene from plants (?)-globuol symbiotic fungi stood formed highly stable complexes with SnocOBP12. By mechanics Poisson–Boltzmann surface area (MM-PBSA) method, calculated free energy three was ?30.572 ± 0.101 kcal/mol, ?28.349 0.119 kcal/mol ?25.244 0.152 respectively. found van der Waals contributed stability complexes. Some were also found: LEU74 TYR109 very important stably bind (?)-?-cedrene, while (E)-?-farnesene, ILE6, MET10, system. We discovered potential ligands analyzed interaction pattern them, this paper provides favorable basis optimizing attractant formulation. Investigation characteristics in olfactory system at level helpful understand behavior develop new methods more effective environmentally friendly