6pxd

<StructureSection load='6pxd' size='340' side='right'caption='[[6pxd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>

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

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxd OCA], [https://pdbe.org/6pxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pxd RCSB], [https://www.ebi.ac.uk/pdbsum/6pxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxd ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/GLRA1_DANRE GLRA1_DANRE]] Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:10188956, PubMed:26344198). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol (By similarity).[UniProtKB:P23415]<ref>PMID:10188956</ref> <ref>PMID:26344198</ref>

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== Publication Abstract from PubMed ==

Ligand-gated ion channels mediate signal transduction at chemical synapses and transition between resting, open, and desensitized states in response to neurotransmitter binding. Neurotransmitters that produce maximum open channel probabilities (Po) are full agonists, whereas those that yield lower than maximum Po are partial agonists. Cys-loop receptors are an important class of neurotransmitter receptors, yet a structure-based understanding of the mechanism of partial agonist action has proven elusive. Here, we study the glycine receptor with the full agonist glycine and the partial agonists taurine and gamma-amino butyric acid (GABA). We use electrophysiology to show how partial agonists populate agonist-bound, closed channel states and cryo-EM reconstructions to illuminate the structures of intermediate, pre-open states, providing insights into previously unseen conformational states along the receptor reaction pathway. We further correlate agonist-induced conformational changes to Po across members of the receptor family, providing a hypothetical mechanism for partial and full agonist action at Cys-loop receptors.

Mechanism of gating and partial agonist action in the glycine receptor.,Yu J, Zhu H, Lape R, Greiner T, Du J, Lu W, Sivilotti L, Gouaux E Cell. 2021 Feb 18;184(4):957-968.e21. doi: 10.1016/j.cell.2021.01.026. Epub 2021 , Feb 9. PMID:33567265<ref>PMID:33567265</ref>

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

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

== References ==

<references/>

[[Category: Du, J]]

[[Category: Gouaux, E]]

[[Category: Lu, W]]

[[Category: Membrane protein]]