Mechanism for Olfactory Receptor-Odorant Interactions
Peter C. Lai, Michael S. Singer, Gordon M. Shepherd, Chiquito J. Crasto
Abstract
Olfactory Receptors (OR) constitutes the human genome's largest gene family. Homology and ab initio modeling techniques have been employed to structurally characterize ORs. We have extended the results of a previous modeling study to understand long term interactions between the OR and ligand. Our results for in vacuo, molecular dynamics simulations of the rat I7 OR model and ten aldehyde ligands indicate that the ligand attempts to periodically exit the binding region of the OR and then reenter it. It also appears that this behavior is periodic as evidenced by dynamical structural changes in the binding pocket as the simulation proceeded. The exit events were strongly correlated with significant structural changes. Our results indicate that the exit-reentry events might be related to the binding strengths of the ligands with the OR from a previous experimental study.
Results
For each simulation run the results show figures of the energy minimized docked position of the ligand, the maximum exit from Lys164 in the binding pocket, a graph of the dynamic characteristics of the ligand and key amino acid residues within the binding pocket and a movie that shows the exit event. Complete movies of the simulation are available by email request from Chiquito Crasto
Ligand Name
PDB formatted file of minimized position of ligand in OR binding pocket
Figure of Minimized Docking Position for the ligand
Figure of "exit" position of the ligand
Graph showing the characteristics of distance and angle behavior of ligand and amino acids in the binding pocket