2xq3: Difference between revisions
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<StructureSection load='2xq3' size='340' side='right'caption='[[2xq3]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='2xq3' size='340' side='right'caption='[[2xq3]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xq3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2xq3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gloeobacter_violaceus_PCC_7421 Gloeobacter violaceus PCC 7421]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQ3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=2xq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xq3 OCA], [https://pdbe.org/2xq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xq3 RCSB], [https://www.ebi.ac.uk/pdbsum/2xq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xq3 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=2xq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xq3 OCA], [https://pdbe.org/2xq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xq3 RCSB], [https://www.ebi.ac.uk/pdbsum/2xq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xq3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gloeobacter violaceus PCC 7421]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bertozzi | [[Category: Bertozzi C]] | ||
[[Category: Dutzler | [[Category: Dutzler R]] | ||
[[Category: Hilf | [[Category: Hilf RJC]] | ||
[[Category: Reiter | [[Category: Reiter A]] | ||
[[Category: Trauner | [[Category: Trauner D]] | ||
[[Category: Zimmermann | [[Category: Zimmermann I]] | ||
Latest revision as of 13:28, 9 May 2024
Pentameric ligand gated ion channel GLIC in complex with Br-lidocainePentameric ligand gated ion channel GLIC in complex with Br-lidocaine
Structural highlights
FunctionGLIC_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 PubMedThe flow of ions through cation-selective members of the pentameric ligand-gated ion channel family is inhibited by a structurally diverse class of molecules that bind to the transmembrane pore in the open state of the protein. To obtain insight into the mechanism of channel block, we have investigated the binding of positively charged inhibitors to the open channel of the bacterial homolog GLIC by using X-ray crystallography and electrophysiology. Our studies reveal the location of two regions for interactions, with larger blockers binding in the center of the membrane and divalent transition metal ions binding to the narrow intracellular pore entry. The results provide a structural foundation for understanding the interactions of the channel with inhibitors that is relevant for the entire family. Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel.,Hilf RJ, Bertozzi C, Zimmermann I, Reiter A, Trauner D, Dutzler R Nat Struct Mol Biol. 2010 Nov;17(11):1330-1336. Epub 2010 Oct 31. PMID:21037567[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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