7m6q
From Proteopedia
(Difference between revisions)
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| - | == | + | ==Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM Tetrahydrocannabinol State 1== |
| - | <StructureSection load='7m6q' size='340' side='right'caption='[[7m6q]]' scene=''> | + | <StructureSection load='7m6q' size='340' side='right'caption='[[7m6q]], [[Resolution|resolution]] 2.91Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M6Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7m6q]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M6Q FirstGlance]. <br> |
| - | </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=7m6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m6q OCA], [https://pdbe.org/7m6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m6q RCSB], [https://www.ebi.ac.uk/pdbsum/7m6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m6q ProSAT]</span></td></tr> | + | </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>, <scene name='pdbligand=TCI:(6AR,10AR)-6,6,9-TRIMETHYL-3-PENTYL-6A,7,8,10A-TETRAHYDRO-6H-BENZO[C]CHROMEN-1-OL'>TCI</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=7m6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m6q OCA], [https://pdbe.org/7m6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m6q RCSB], [https://www.ebi.ac.uk/pdbsum/7m6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m6q ProSAT]</span></td></tr> | ||
</table> | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Glycine receptors (GlyRs) are key players in mediating fast inhibitory neurotransmission at these synapses. While previous high-resolution structures have provided insights into the molecular architecture of GlyR, several mechanistic questions pertaining to channel function are still unanswered. Here, we present Cryo-EM structures of the full-length GlyR protein complex reconstituted into lipid nanodiscs that are captured in the unliganded (closed), glycine-bound (open and desensitized), and allosteric modulator-bound conformations. A comparison of these states reveals global conformational changes underlying GlyR channel gating and modulation. The functional state assignments were validated by molecular dynamics simulations, and the observed permeation events are in agreement with the anion selectivity and conductance of GlyR. These studies provide the structural basis for gating, ion selectivity, and single-channel conductance properties of GlyR in a lipid environment. | ||
| + | |||
| + | Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs.,Kumar A, Basak S, Rao S, Gicheru Y, Mayer ML, Sansom MSP, Chakrapani S Nat Commun. 2020 Jul 27;11(1):3752. doi: 10.1038/s41467-020-17364-5. PMID:32719334<ref>PMID:32719334</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7m6q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chakrapani S]] | + | [[Category: Chakrapani, S]] |
| - | [[Category: Kumar A]] | + | [[Category: Kumar, A]] |
| + | [[Category: Glycine receptor recombinant protein]] | ||
| + | [[Category: Ions ligands receptor]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 05:07, 10 August 2022
Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM Tetrahydrocannabinol State 1
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