Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor

Sandip Basak; Yvonne Gicheru; Abhijeet Kapoor; Megan L. Mayer; Marta Filizola; Sudha Chakrapani

doi:10.1038/s41467-019-11142-8

Nature Communications (Jul 2019)

Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor

Sandip Basak,
Yvonne Gicheru,
Abhijeet Kapoor,
Megan L. Mayer,
Marta Filizola,
Sudha Chakrapani

Affiliations

Sandip Basak: Department of Physiology and Biophysics, Case Western Reserve University
Yvonne Gicheru: Department of Physiology and Biophysics, Case Western Reserve University
Abhijeet Kapoor: Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai
Megan L. Mayer: Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Stanford University
Marta Filizola: Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai
Sudha Chakrapani: Department of Physiology and Biophysics, Case Western Reserve University

DOI: https://doi.org/10.1038/s41467-019-11142-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

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Serotonin receptors (5-HT3R) belong to the pentameric ligand-gated ion channel superfamily and mediate excitatory postsynaptic signaling. Here the authors present the high-resolution cryo-EM structure of 5-HT3AR bound with the competitive antagonist granisetron and further validate the granisetron-binding mode with electrophysiology measurements and MD simulations.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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