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| | ==The GLIC pentameric Ligand-Gated Ion Channel 2-21' cross-linked mutant complexed to bromoform== | | ==The GLIC pentameric Ligand-Gated Ion Channel 2-21' cross-linked mutant complexed to bromoform== |
| - | <StructureSection load='5hcm' size='340' side='right' caption='[[5hcm]], [[Resolution|resolution]] 3.15Å' scene=''> | + | <StructureSection load='5hcm' size='340' side='right'caption='[[5hcm]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hcm]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Glovo Glovo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HCM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hcm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gloeobacter_violaceus Gloeobacter violaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HCM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MBR:TRIBROMOMETHANE'>MBR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glvI, glr4197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33072 GLOVO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MBR:TRIBROMOMETHANE'>MBR</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hcm OCA], [http://pdbe.org/5hcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hcm RCSB], [http://www.ebi.ac.uk/pdbsum/5hcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hcm ProSAT]</span></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=5hcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hcm OCA], [https://pdbe.org/5hcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hcm RCSB], [https://www.ebi.ac.uk/pdbsum/5hcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hcm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI]] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.<ref>PMID:17167423</ref> | + | [https://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.<ref>PMID:17167423</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5hcm" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5hcm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glovo]] | + | [[Category: Gloeobacter violaceus]] |
| - | [[Category: Delarue, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Sauguet, L]] | + | [[Category: Delarue M]] |
| - | [[Category: Shahsavar, A]] | + | [[Category: Sauguet L]] |
| - | [[Category: Anaesthetic]] | + | [[Category: Shahsavar A]] |
| - | [[Category: Ion channel]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
GLIC_GLOVI Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.[1]
Publication Abstract from PubMed
Pentameric ligand-gated ion channels have been identified as the principal target of general anesthetics (GA), whose molecular mechanism of action remains poorly understood. Bacterial homologs, such as the Gloeobacter violaceus receptor (GLIC), have been shown to be valid functional models of GA action. The GA bromoform inhibits GLIC at submillimolar concentration. We characterize bromoform binding by crystallography and molecular dynamics (MD) simulations. GLIC's open form structure identified three intra-subunit binding sites. We crystallized the locally closed form with an additional bromoform molecule in the channel pore. We systematically compare binding with the multiple potential sites of allosteric channel regulation in the open, locally closed, and resting forms. MD simulations reveal differential exchange pathways between sites from one form to the other. GAs predominantly access the receptor from the lipid bilayer in all cases. Differential binding affinity among the channel forms is observed; the pore site markedly stabilizes the inactive versus active state.
Sites of Anesthetic Inhibitory Action on a Cationic Ligand-Gated Ion Channel.,Laurent B, Murail S, Shahsavar A, Sauguet L, Delarue M, Baaden M Structure. 2016 Apr 5;24(4):595-605. doi: 10.1016/j.str.2016.02.014. Epub 2016, Mar 24. PMID:27021161[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bocquet N, Prado de Carvalho L, Cartaud J, Neyton J, Le Poupon C, Taly A, Grutter T, Changeux JP, Corringer PJ. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature. 2007 Jan 4;445(7123):116-9. Epub 2006 Dec 10. PMID:17167423 doi:10.1038/nature05371
- ↑ Laurent B, Murail S, Shahsavar A, Sauguet L, Delarue M, Baaden M. Sites of Anesthetic Inhibitory Action on a Cationic Ligand-Gated Ion Channel. Structure. 2016 Apr 5;24(4):595-605. doi: 10.1016/j.str.2016.02.014. Epub 2016, Mar 24. PMID:27021161 doi:http://dx.doi.org/10.1016/j.str.2016.02.014
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