WIKIMEDIA, TOKINOResearchers at the Vollum Institute in Portland, Oregon, have resolved the crystal structures of the human serotonin transporter (SERT) bound to two different antidepressant drugs. The structures show where the drugs bind, how they inhibit transporter function, and offer insights for the design and development of new psychiatric pharmaceuticals.
“There are no other human transporters in this family that have been crystallized and where we know the structure, so [the paper] is a milestone in that sense,” said pharmacologist Gary Rudnick of Yale University who was not involved in the study. “The structure can be used to understand details about the way the protein works, the way it binds ligands [and] for drug development,” he added.
Serotonin is a neurotransmitter that influences neurological systems such as mood, sleep, cognition, and hunger. Selective serotonin reuptake inhibitors (SSRIs) are drugs that prolong the presence, and thus activity, of serotonin in neural synapses, and are used in the treatment of depression, anxiety and other related disorders. They work by binding and inactivating SERT, which normally transports serotonin ...
