Cryo-EM structure of 5-HT3A receptor in its resting conformation

Sandip Basak, Yvonne Gicheru, Amrita Samanta, Sudheer Kumar Molugu, Wei Huang, Maria la de Fuente, Taylor Hughes, Derek J. Taylor, Marvin T. Nieman, Vera Moiseenkova-Bell and Sudha Chakrapani ()
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Sandip Basak: Case Western Reserve University
Yvonne Gicheru: Case Western Reserve University
Amrita Samanta: Case Western Reserve University
Sudheer Kumar Molugu: Case Western Reserve University
Wei Huang: Case Western Reserve University
Maria la de Fuente: Case Western Reserve University
Taylor Hughes: Case Western Reserve University
Derek J. Taylor: Case Western Reserve University
Marvin T. Nieman: Case Western Reserve University
Vera Moiseenkova-Bell: Case Western Reserve University
Sudha Chakrapani: Case Western Reserve University

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract Serotonin receptors (5-HT3AR) directly regulate gut movement, and drugs that inhibit 5-HT3AR function are used to control emetic reflexes associated with gastrointestinal pathologies and cancer therapies. The 5-HT3AR 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-HT3AR 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-HT3AR crystal structure, the full-length channel in the apo-conformation adopts a more expanded conformation of all the three domains with a characteristic twist that is implicated in gating.

Date: 2018
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DOI: 10.1038/s41467-018-02997-4

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