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[[ | ==PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH TETRABUTYLANTIMONY (TBSB)== | ||
<StructureSection load='2xqa' size='340' side='right' caption='[[2xqa]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xqa]] is a 5 chain structure with sequence from [http://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=2XQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XQA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SB:ANTIMONY+(III)+ION'>SB</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xq7|2xq7]], [[2xq9|2xq9]], [[2xq5|2xq5]], [[2xq3|2xq3]], [[2xq8|2xq8]], [[2xq4|2xq4]], [[2xq6|2xq6]]</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=2xqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xqa RCSB], [http://www.ebi.ac.uk/pdbsum/2xqa PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:21037567</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels|Ion channels]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gloeobacter violaceus pcc 7421]] | [[Category: Gloeobacter violaceus pcc 7421]] | ||
[[Category: Bertozzi, C.]] | [[Category: Bertozzi, C.]] | ||
Revision as of 16:07, 22 October 2014
PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH TETRABUTYLANTIMONY (TBSB)PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH TETRABUTYLANTIMONY (TBSB)
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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