4pa4: Difference between revisions
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''' | ==Structure of NavMS in complex with channel blocking compound== | ||
<StructureSection load='4pa4' size='340' side='right' caption='[[4pa4]], [[Resolution|resolution]] 3.02Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pa4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PA4 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbc|4cbc]], [[4p90|4p90]], [[4p2z|4p2z]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pa4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pa4 RCSB], [http://www.ebi.ac.uk/pdbsum/4pa4 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Voltage-gated sodium channels are important targets for the development of pharmaceutical drugs, because mutations in different human sodium channel isoforms have causal relationships with a range of neurological and cardiovascular diseases. In this study, functional electrophysiological studies show that the prokaryotic sodium channel from Magnetococcus marinus (NavMs) binds and is inhibited by eukaryotic sodium channel blockers in a manner similar to the human Nav1.1 channel, despite millions of years of divergent evolution between the two types of channels. Crystal complexes of the NavMs pore with several brominated blocker compounds depict a common antagonist binding site in the cavity, adjacent to lipid-facing fenestrations proposed to be the portals for drug entry. In silico docking studies indicate the full extent of the blocker binding site, and electrophysiology studies of NavMs channels with mutations at adjacent residues validate the location. These results suggest that the NavMs channel can be a valuable tool for screening and rational design of human drugs. | |||
Prokaryotic NavMs channel as a structural and functional model for eukaryotic sodium channel antagonism.,Bagneris C, DeCaen PG, Naylor CE, Pryde DC, Nobeli I, Clapham DE, Wallace BA Proc Natl Acad Sci U S A. 2014 May 21. pii: 201406855. PMID:24850863<ref>PMID:24850863</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bagneris, C.]] | |||
[[Category: Naylor, C E.]] | |||
[[Category: Wallace, B A.]] | |||
[[Category: Channel blocking compound]] | |||
[[Category: Membrane protein]] | |||
[[Category: Pore]] | |||
[[Category: Sodium channel]] | |||
[[Category: Transport protein]] | |||