4cbc - Revision history

OCA at 12:07, 20 December 2023

2023-12-20T12:07:03Z

← Older revision		Revision as of 12:07, 20 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetococcus_marinus_MC-1 Magnetococcus marinus MC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetococcus_marinus_MC-1 Magnetococcus marinus MC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.664Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [https://pdbe.org/4cbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [https://www.ebi.ac.uk/pdbsum/4cbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbc 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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [https://pdbe.org/4cbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [https://www.ebi.ac.uk/pdbsum/4cbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/A0L5S6_MAGMM A0L5S6_MAGMM]]		[https://www.uniprot.org/uniprot/A0L5S6_MAGMM A0L5S6_MAGMM]
			<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>
			<div class="pdbe-citations 4cbc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Ion channels 3D structures\|Ion channels 3D structures]]		*[[Ion channels 3D structures\|Ion channels 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:36, 7 September 2022

2022-09-07T17:36:37Z

← Older revision		Revision as of 17:36, 7 September 2022
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	<StructureSection load='4cbc' size='340' side='right'caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>		<StructureSection load='4cbc' size='340' side='right'caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CBC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetococcus_marinus_MC-1 Magnetococcus marinus MC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cal\|4cal]], [[4cbd\|4cbd]]~~</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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [https://pdbe.org/4cbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [https://www.ebi.ac.uk/pdbsum/4cbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbc ProSAT]</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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [~~http~~://pdbe.org/4cbc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cbc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbc ProSAT]</span></td></tr>
	</table>		</table>
	~~<div style="background-color:#fffaf0;">~~		== Function ==
	== ~~Publication Abstract from PubMed~~ ==		[[https://www.uniprot.org/uniprot/A0L5S6_MAGMM A0L5S6_MAGMM]]
	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>		==See Also==
			*[[Ion channels 3D structures\|Ion channels 3D structures]]
	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4cbc" style="background-color:#fffaf0;"></div>~~
	== ~~References~~ ==
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Bagneris, C~~]]		[[Category: Magnetococcus marinus MC-1]]
	[[Category: ~~Naylor,~~ C E]]		[[Category: Bagneris C]]
	[[Category: ~~Wallace, B A~~]]		[[Category: Naylor CE]]
	[[Category: ~~Membrane protein]]~~		[[Category: Wallace BA]]
	~~[[Category: Selectivity filter]]~~
	~~[[Category: Sodium channel]]~~
	~~[[Category: Transport protein~~]]

OCA at 06:55, 10 July 2019

2019-07-10T06:55:30Z

← Older revision		Revision as of 06:55, 10 July 2019
Line 1:		Line 1:

	==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==		==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==
	<StructureSection load='4cbc' size='340' side='right' caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>		<StructureSection load='4cbc' size='340' side='right'caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBC FirstGlance]. <br>
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Bagneris, C]]		[[Category: Bagneris, C]]
	[[Category: Naylor, C E]]		[[Category: Naylor, C E]]

OCA at 14:18, 11 August 2016

2016-08-11T14:18:27Z

← Older revision		Revision as of 14:18, 11 August 2016
Line 1:		Line 1:

	==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==		==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==
	<StructureSection load='4cbc' size='340' side='right' caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>		<StructureSection load='4cbc' size='340' side='right' caption='[[4cbc]], [[Resolution\|resolution]] 2.66Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cal\|4cal]], [[4cbd\|4cbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cal\|4cal]], [[4cbd\|4cbd]]</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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [http://www.ebi.ac.uk/pdbsum/4cbc 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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [http://pdbe.org/4cbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [http://www.ebi.ac.uk/pdbsum/4cbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbc ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4cbc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:26, 4 January 2015

2015-01-04T12:26:43Z

← Older revision		Revision as of 12:26, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cal\|4cal]], [[4cbd\|4cbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cal\|4cal]], [[4cbd\|4cbd]]</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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [http://www.ebi.ac.uk/pdbsum/4cbc 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=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [http://www.ebi.ac.uk/pdbsum/4cbc PDBsum]</span></td></tr>
	<table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bagneris, C.]]		[[Category: Bagneris, C]]
	[[Category: Naylor, C E.]]		[[Category: Naylor, C E]]
	[[Category: Wallace, B A.]]		[[Category: Wallace, B A]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
	[[Category: Selectivity filter]]		[[Category: Selectivity filter]]
	[[Category: Sodium channel]]		[[Category: Sodium channel]]
	[[Category: Transport protein]]		[[Category: Transport protein]]

OCA at 05:21, 25 June 2014

2014-06-25T05:21:06Z

← Older revision		Revision as of 05:21, 25 June 2014
Line 13:		Line 13:
	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>		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 ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==

OCA at 04:37, 4 June 2014

2014-06-04T04:37:52Z

← Older revision		Revision as of 04:37, 4 June 2014
Line 9:		Line 9:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Voltage-gated ~~sodium channels have essential roles in electrical signalling. Prokaryotic~~ sodium channels are ~~tetramers consisting~~ of ~~transmembrane (TM) voltage-sensing and pore domains~~, ~~and~~ a ~~cytoplasmic carboxy-terminal domain. Previous crystal structures~~ of ~~bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs)~~. ~~Here~~, ~~using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we~~ show that the ~~CTD of the NavMs~~ channel from Magnetococcus marinus ~~includes~~ a ~~flexible region linking~~ the ~~TM domains to a four-helix coiled-coil bundle~~. ~~A 2~~.~~9 A resolution crystal structure~~ of the NavMs pore ~~indicates~~ the ~~position~~ of the ~~CTD~~, ~~which is consistent~~ with the ~~EPR-derived structure~~. ~~Functional analyses demonstrate~~ that the ~~coiled-coil domain couples inactivation with~~ channel ~~opening,~~ and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of ~~the coiled-coil~~.		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.

	~~Role of the C-terminal domain in the structure~~ and ~~function of tetrameric~~ sodium ~~channels~~.,Bagneris C, ~~Decaen~~ PG~~, Hall BA~~, Naylor CE, Clapham DE~~, Kay CW~~, Wallace BA ~~Nat Commun~~. ~~2013 Sep 20;4:2465~~. ~~doi~~: ~~10.1038/ncomms3465~~. PMID:~~24051986~~<ref>PMID:~~24051986~~</ref>		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 MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>

OCA at 09:44, 28 May 2014

2014-05-28T09:44:48Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==
-The entry 4cbc is ON HOLD  until Paper Publication
+Role of the C-terminal domain in the structure and function of tetrameric sodium channels.,Bagneris C, Decaen PG, Hall BA, Naylor CE, Clapham DE, Kay CW, Wallace BA Nat Commun. 2013 Sep 20;4:2465. doi: 10.1038/ncomms3465. PMID:24051986<ref>PMID:24051986</ref>
-Authors: Bagneris, C., Naylor, C.E., Wallace, B.A.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak
+== References ==

OCA at 06:46, 19 March 2014

2014-03-19T06:46:02Z

← Older revision		Revision as of 06:46, 19 March 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4cbc is ON HOLD		The entry 4cbc is ON HOLD until Paper Publication

	Authors: Bagneris, C., Naylor, C.E., Wallace, B.A.		Authors: Bagneris, C., Naylor, C.E., Wallace, B.A.

	Description: Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak		Description: Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak

OCA: Protected "4cbc" [edit=sysop:move=sysop]

2013-10-23T05:39:53Z

Protected "4cbc" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:39, 23 October 2013
(No difference)