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6Y5A

Serotonin-bound 5-HT3A receptor in Salipro

Summary for 6Y5A
Entry DOI10.2210/pdb6y5a/pdb
Related6Y59 6Y5B
EMDB information10691 10692 10693
Descriptor5-hydroxytryptamine receptor 3A, SEROTONIN (2 entities in total)
Functional Keywordspentameric ligand-gated ion channel, plgic, serotonin 5-ht3a receptor, serotonin, agonist-bound, salipro, membrane protein
Biological sourceMus musculus (House mouse)
Total number of polymer chains5
Total formula weight304221.51
Authors
Zhang, Y.,Dijkman, P.M.,Zou, R.,Zandl-Lang, M.,Sanchez, R.M.,Eckhardt-Strelau, L.,Koefeler, H.,Vogel, H.,Yuan, S.,Kudryashev, M. (deposition date: 2020-02-25, release date: 2020-12-23, Last modification date: 2024-10-23)
Primary citationZhang, Y.,Dijkman, P.M.,Zou, R.,Zandl-Lang, M.,Sanchez, R.M.,Eckhardt-Strelau, L.,Kofeler, H.,Vogel, H.,Yuan, S.,Kudryashev, M.
Asymmetric opening of the homopentameric 5-HT 3A serotonin receptor in lipid bilayers.
Nat Commun, 12:1074-1074, 2021
Cited by
PubMed Abstract: Pentameric ligand-gated ion channels (pLGICs) of the Cys-loop receptor family are key players in fast signal transduction throughout the nervous system. They have been shown to be modulated by the lipid environment, however the underlying mechanism is not well understood. We report three structures of the Cys-loop 5-HT serotonin receptor (5HTR) reconstituted into saposin-based lipid bilayer discs: a symmetric and an asymmetric apo state, and an asymmetric agonist-bound state. In comparison to previously published 5HTR conformations in detergent, the lipid bilayer stabilises the receptor in a more tightly packed, 'coupled' state, involving a cluster of highly conserved residues. In consequence, the agonist-bound receptor conformation adopts a wide-open pore capable of conducting sodium ions in unbiased molecular dynamics (MD) simulations. Taken together, we provide a structural basis for the modulation of 5HTR by the membrane environment, and a model for asymmetric activation of the receptor.
PubMed: 33594077
DOI: 10.1038/s41467-021-21016-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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