6y5a

<table><tr><td colspan='2'>[[6y5a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y5A FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SRO:SEROTONIN'>SRO</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6y59|6y59]], [[6y5b|6y5b]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Htr3a, 5ht3, Htr3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/5HT3A_MOUSE 5HT3A_MOUSE]] This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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-HT3A serotonin receptor (5HT3R) 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 5HT3R 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 5HT3R by the membrane environment, and a model for asymmetric activation of the receptor.

Asymmetric opening of the homopentameric 5-HT3A serotonin receptor in lipid bilayers.,Zhang Y, Dijkman PM, Zou R, Zandl-Lang M, Sanchez RM, Eckhardt-Strelau L, Kofeler H, Vogel H, Yuan S, Kudryashev M Nat Commun. 2021 Feb 16;12(1):1074. doi: 10.1038/s41467-021-21016-7. PMID:33594077<ref>PMID:33594077</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 6y5a" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Dijkman, P M]]

[[Category: Eckhardt-Strelau, L]]

[[Category: Koefeler, H]]

[[Category: Kudryashev, M]]

[[Category: Sanchez, R M]]

[[Category: Vogel, H]]

[[Category: Yuan, S]]

[[Category: Zandl-Lang, M]]

[[Category: Zhang, Y]]

[[Category: Zou, R]]

[[Category: Serotonin 5-ht3a receptor]]