9y95: Difference between revisions

Latest revision as of 07:51, 19 March 2026

Homomeric Glycine Receptor alpha2 with PTX in an Apo State

Structural highlights

9y95 is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.45Å
Ligands:	NAG, PX4, RI5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

GLRA2_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

GLRA2_HUMAN Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15302677, PubMed:16144831, PubMed:2155780, PubMed:23895467, PubMed:25445488, PubMed:26370147, PubMed:34473954). Channel opening is also triggered by taurine and beta-alanine (PubMed:15302677). Plays a role in synaptic plasticity (By similarity). Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability (PubMed:25445488). Plays a role in cellular responses to ethanol (PubMed:23895467).[UniProtKB:Q7TNC8]^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Miller PS, Harvey RJ, Smart TG. Differential agonist sensitivity of glycine receptor alpha2 subunit splice variants. Br J Pharmacol. 2004 Sep;143(1):19-26. PMID:15302677 doi:10.1038/sj.bjp.0705875
↑ Miller PS, Da Silva HM, Smart TG. Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors. J Biol Chem. 2005 Nov 11;280(45):37877-84. PMID:16144831 doi:10.1074/jbc.M508303200
↑ Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H. Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 1990 Mar;9(3):771-6. PMID:2155780 doi:10.1002/j.1460-2075.1990.tb08172.x
↑ McCracken LM, Trudell JR, McCracken ML, Harris RA. Zinc-dependent modulation of α2 Alcohol Clin Exp Res. 2013 Dec;37(12):2002-10. PMID:23895467 doi:10.1111/acer.12192
↑ Zhang Y, Dixon CL, Keramidas A, Lynch JW. Functional reconstitution of glycinergic synapses incorporating defined glycine receptor subunit combinations. Neuropharmacology. 2015 Feb;89:391-7. PMID:25445488 doi:10.1016/j.neuropharm.2014.10.026
↑ Yu H, Bai XC, Wang W. Characterization of the subunit composition and structure of adult human glycine receptors. Neuron. 2021 Sep 1;109(17):2707-2716.e6. PMID:34473954 doi:10.1016/j.neuron.2021.08.019

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Miller PS, Harvey RJ, Smart TG. Differential agonist sensitivity of glycine receptor alpha2 subunit splice variants. Br J Pharmacol. 2004 Sep;143(1):19-26. PMID:15302677 doi:10.1038/sj.bjp.0705875

[2] Miller PS, Da Silva HM, Smart TG. Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors. J Biol Chem. 2005 Nov 11;280(45):37877-84. PMID:16144831 doi:10.1074/jbc.M508303200

[3] Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H. Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 1990 Mar;9(3):771-6. PMID:2155780 doi:10.1002/j.1460-2075.1990.tb08172.x

[4] McCracken LM, Trudell JR, McCracken ML, Harris RA. Zinc-dependent modulation of α2 Alcohol Clin Exp Res. 2013 Dec;37(12):2002-10. PMID:23895467 doi:10.1111/acer.12192

[5] Zhang Y, Dixon CL, Keramidas A, Lynch JW. Functional reconstitution of glycinergic synapses incorporating defined glycine receptor subunit combinations. Neuropharmacology. 2015 Feb;89:391-7. PMID:25445488 doi:10.1016/j.neuropharm.2014.10.026

[6] Yu H, Bai XC, Wang W. Characterization of the subunit composition and structure of adult human glycine receptors. Neuron. 2021 Sep 1;109(17):2707-2716.e6. PMID:34473954 doi:10.1016/j.neuron.2021.08.019

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9y95 is ON HOLD  until Paper Publication
+==Homomeric Glycine Receptor alpha2 with PTX in an Apo State==
+<StructureSection load='9y95' size='340' side='right'caption='[[9y95]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9y95]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Y95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Y95 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.45&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene>, <scene name='pdbligand=RI5:(1AR,2AR,3S,6R,6AS,8AS,8BR,9R)-2A-HYDROXY-8B-METHYL-9-(PROP-1-EN-2-YL)HEXAHYDRO-3,6-METHANO-1,5,7-TRIOXACYCLOPENTA[IJ]CYCLOPROPA[A]AZULENE-4,8(3H)-DIONE'>RI5</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=9y95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9y95 OCA], [https://pdbe.org/9y95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9y95 RCSB], [https://www.ebi.ac.uk/pdbsum/9y95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9y95 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/GLRA2_HUMAN GLRA2_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/GLRA2_HUMAN GLRA2_HUMAN] Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15302677, PubMed:16144831, PubMed:2155780, PubMed:23895467, PubMed:25445488, PubMed:26370147, PubMed:34473954). Channel opening is also triggered by taurine and beta-alanine (PubMed:15302677). Plays a role in synaptic plasticity (By similarity). Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability (PubMed:25445488). Plays a role in cellular responses to ethanol (PubMed:23895467).[UniProtKB:Q7TNC8]<ref>PMID:15302677</ref> <ref>PMID:16144831</ref> <ref>PMID:2155780</ref> <ref>PMID:23895467</ref> <ref>PMID:25445488</ref> <ref>PMID:34473954</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chakrapani S]]
+[[Category: Gibbs E]]
+[[Category: Klemm E]]

9y95: Difference between revisions

Latest revision as of 07:51, 19 March 2026

Homomeric Glycine Receptor alpha2 with PTX in an Apo State

Structural highlights

Disease

Function

References

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