Cryo-EM structure of 5-HT_3A receptor in its resting conformation.

ABSTRACT: Serotonin receptors (5-HT_3AR) directly regulate gut movement, and drugs that inhibit 5-HT_3AR function are used to control emetic reflexes associated with gastrointestinal pathologies and cancer therapies. The 5-HT_3AR function involves a finely tuned orchestration of three domain movements that include the ligand-binding domain, the pore domain, and the intracellular domain. Here, we present the structure from the full-length 5-HT_3AR channel in the apo-state determined by single-particle cryo-electron microscopy at a nominal resolution of 4.3 Å. In this conformation, the ligand-binding domain adopts a conformation reminiscent of the unliganded state with the pore domain captured in a closed conformation. In comparison to the 5-HT_3AR cry

SUBMITTER: Basak S 

PROVIDER: S-EPMC5802770 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature