Conformational transitions of the serotonin 5-HT<sub>3</sub> receptor.
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ABSTRACT: The serotonin 5-HT3 receptor is a pentameric ligand-gated ion channel (pLGIC). It belongs to a large family of receptors that function as allosteric signal transducers across the plasma membrane1,2; upon binding of neurotransmitter molecules to extracellular sites, the receptors undergo complex conformational transitions that result in transient opening of a pore permeable to ions. 5-HT3 receptors are therapeutic targets for emesis and nausea, irritable bowel syndrome and depression3. In spite of several reported pLGIC structures4-8, no clear unifying view has emerged on the conformational transitions involved in channel gating. Here we report four cryo-electron microscopy structures of the full-length mouse 5-HT3 receptor i
SUBMITTER: Polovinkin L
PROVIDER: S-EPMC6614044 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
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