Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter.

ABSTRACT: Uptake of neurotransmitters by sodium-coupled monoamine transporters of the NSS family is required for termination of synaptic transmission. Transport is tightly regulated by protein-protein interactions involving the small cytoplasmic segments at the amino- and carboxy-terminal ends of the transporter. Although structures of homologues provide information about the transmembrane regions of these transporters, the structural arrangement of the terminal domains remains largely unknown. Here, we combined molecular modeling, biochemical, and biophysical approaches in an iterative manner to investigate the structure of the 82-residue N-terminal and 30-residue C-terminal domains of human serotonin transporter (SERT). Several secondary structures were predicted in these domains, and structural m

SUBMITTER: Fenollar-Ferrer C 

PROVIDER: S-EPMC4147951 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature