Dopamine is a key neurotransmitter in the brain involved in many processes, including motor control, reward, and cognition. The dopamine transporter (DAT) is a membrane protein responsible for the uptake of dopamine, thus terminating its function. DAT is a key target for drugs treating Parkinson, ADHD, mood disorders, and schizophrenia, and inhibition of DAT is a central mechanism for drugs such as cocaine. Our collaborators in the Gouaux lab at OHSU have captured the structure of human DAT using cryoEM, together with a competitive inhibitor at its central binding site, and an allosteric inhibitor in an external site. However, the precise binding poses and stability of these inhibitors were unclear. To address these issues, the Resource researchers applied molecular dynamics simulations with NAMD/AMBER and analyzed by VMD to explore the most likely binding poses and stability of the inhibitors. For more details, see our recent publication in Nature.