2xq5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<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=2xq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xq5 RCSB], [http://www.ebi.ac.uk/pdbsum/2xq5 PDBsum]</span></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=2xq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xq5 RCSB], [http://www.ebi.ac.uk/pdbsum/2xq5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q7NDN8_GLOVI Q7NDN8_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 == | ||
| Line 23: | Line 25: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gloeobacter violaceus pcc 7421]] | [[Category: Gloeobacter violaceus pcc 7421]] | ||
[[Category: Bertozzi, C | [[Category: Bertozzi, C]] | ||
[[Category: Dutzler, R | [[Category: Dutzler, R]] | ||
[[Category: Hilf, R J.C | [[Category: Hilf, R J.C]] | ||
[[Category: Reiter, A | [[Category: Reiter, A]] | ||
[[Category: Trauner, D | [[Category: Trauner, D]] | ||
[[Category: Zimmermann, I | [[Category: Zimmermann, I]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Open channel block]] | [[Category: Open channel block]] | ||
Revision as of 11:27, 25 December 2014
PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH TETRAETHYLARSONIUM (TEAS)PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH TETRAETHYLARSONIUM (TEAS)
Structural highlights
Function[Q7NDN8_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
|
| ||||||||||||||||||