5bkf: Difference between revisions

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New page: '''Unreleased structure''' The entry 5bkf is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5bkf is ON HOLD
==Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized state==
<StructureSection load='5bkf' size='340' side='right'caption='[[5bkf]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bkf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BKF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</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=5bkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bkf OCA], [https://pdbe.org/5bkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bkf RCSB], [https://www.ebi.ac.uk/pdbsum/5bkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bkf 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>


Authors:  
==See Also==
 
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Aequorea victoria]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Wang W]]
[[Category: Yu H]]

Latest revision as of 06:52, 21 November 2024

Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized stateCyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized state

Structural highlights

5bkf is a 5 chain structure with sequence from Aequorea victoria and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.6Å
Ligands:,
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]

See Also

References

  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

5bkf, resolution 3.60Å

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