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6plq

From Proteopedia

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Current revision

CryoEM structure of zebra fish alpha-1 glycine receptor YGF mutant bound with GABA in SMA, super-open state

Structural highlights

6plq is a 5 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.4Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ David-Watine B, Goblet C, de Saint Jan D, Fucile S, Devignot V, Bregestovski P, Korn H. Cloning, expression and electrophysiological characterization of glycine receptor alpha subunit from zebrafish. Neuroscience. 1999 Apr;90(1):303-17. doi: 10.1016/s0306-4522(98)00430-8. PMID:10188956 doi:http://dx.doi.org/10.1016/s0306-4522(98)00430-8
↑ Du J, Lu W, Wu S, Cheng Y, Gouaux E. Glycine receptor mechanism elucidated by electron cryo-microscopy. Nature. 2015 Sep 7. doi: 10.1038/nature14853. PMID:26344198 doi:http://dx.doi.org/10.1038/nature14853
↑ Yu J, Zhu H, Lape R, Greiner T, Du J, Lu W, Sivilotti L, Gouaux E. Mechanism of gating and partial agonist action in the glycine receptor. Cell. 2021 Feb 18;184(4):957-968.e21. doi: 10.1016/j.cell.2021.01.026. Epub 2021 , Feb 9. PMID:33567265 doi:http://dx.doi.org/10.1016/j.cell.2021.01.026

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6plq"

Categories: Danio rerio | Large Structures | Gouaux E | Yu J | Zhu H

@@ Line 3: / Line 3: @@
 <StructureSection load='6plq' size='340' side='right'caption='[[6plq]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6plq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PLQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6plq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PLQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glra1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=6plq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6plq OCA], [https://pdbe.org/6plq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6plq RCSB], [https://www.ebi.ac.uk/pdbsum/6plq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6plq ProSAT]</span></td></tr>
 </table>
 == 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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Brachidanio rerio]]
+[[Category: Danio rerio]]
 [[Category: Large Structures]]
-[[Category: Gouaux, E]]
+[[Category: Gouaux E]]
-[[Category: Yu, J]]
+[[Category: Yu J]]
-[[Category: Zhu, H]]
+[[Category: Zhu H]]
-[[Category: Cryoem]]
-[[Category: Glycine receptor]]
-[[Category: Membrane protein]]
-[[Category: Sma]]

6plq

From Proteopedia

Current revision

CryoEM structure of zebra fish alpha-1 glycine receptor YGF mutant bound with GABA in SMA, super-open state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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