1g1z - Revision history

OCA at 18:36, 29 November 2023

OCA — Wed, 29 Nov 2023 18:36:51 GMT

←Older revision		Revision as of 18:36, 29 November 2023
Line 1:		Line 1:

	==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==		==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==
-	<StructureSection load='1g1z' size='340' side='right'caption='[[1g1z~~]], [[NMR_Ensembles_of_Models \| 18 NMR models~~]]' scene=''>	+	<StructureSection load='1g1z' size='340' side='right'caption='[[1g1z]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_ermineus Conus ermineus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height~~: ~~3em;~~'>~~[[1g1p\|1g1p]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [https://pdbe.org/1g1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [https://www.ebi.ac.uk/pdbsum/1g1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [https://pdbe.org/1g1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [https://www.ebi.ac.uk/pdbsum/1g1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CO6A_CONER CO6A_CONER]~~] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.	+	[https://www.uniprot.org/uniprot/U6A_CONER U6A_CONER] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.<ref>PMID:14615484</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Conus ermineus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Gall, F Le~~]]	+	[[Category: Lamthanh H]]
-	[[Category: ~~Lamthanh, H~~]]	+	[[Category: Lancelin JM]]
-	[[Category: ~~Lancelin, J M~~]]	+	[[Category: Le Gall F]]
-	[[Category: Menez, A]]	+	[[Category: Menez A]]
-	[[Category: Volpon, L]]	+	[[Category: Volpon L]]
-	~~[[Category: Cis/trans isomerism of leu12-pro13 peptide bond]]~~	+
-	~~[[Category: Hydroxyproline]]~~	+
-	~~[[Category: Three disulfide linkage]]~~	+
-	~~[[Category: Toxin~~]]	+

OCA at 07:10, 24 March 2021

OCA — Wed, 24 Mar 2021 07:10:47 GMT

←Older revision		Revision as of 07:10, 24 March 2021
Line 3:		Line 3:
	<StructureSection load='1g1z' size='340' side='right'caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>		<StructureSection load='1g1z' size='340' side='right'caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g1p\|1g1p]]</div></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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [~~http~~://pdbe.org/1g1z PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1g1z PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [https://pdbe.org/1g1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [https://www.ebi.ac.uk/pdbsum/1g1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CO6A_CONER CO6A_CONER]] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.	+	[[https://www.uniprot.org/uniprot/CO6A_CONER CO6A_CONER]] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:37, 19 June 2019

OCA — Wed, 19 Jun 2019 07:37:32 GMT

←Older revision		Revision as of 07:37, 19 June 2019
Line 1:		Line 1:

	==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==		==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==
-	<StructureSection load='1g1z' size='340' side='right' caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>	+	<StructureSection load='1g1z' size='340' side='right'caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Gall, F Le]]		[[Category: Gall, F Le]]
	[[Category: Lamthanh, H]]		[[Category: Lamthanh, H]]

OCA at 10:59, 13 September 2017

OCA — Wed, 13 Sep 2017 10:59:01 GMT

←Older revision		Revision as of 10:59, 13 September 2017
Line 1:		Line 1:
		+
	==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==		==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==
	<StructureSection load='1g1z' size='340' side='right' caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>		<StructureSection load='1g1z' size='340' side='right' caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://pdbe.org/1g1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://pdbe.org/1g1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 22:13, 10 September 2015

OCA — Thu, 10 Sep 2015 22:13:25 GMT

←Older revision		Revision as of 22:13, 10 September 2015
Line 5:		Line 5:
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://pdbe.org/1g1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~CXD6A_CONER CXD6A_CONER~~]] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.	+	[[http://www.uniprot.org/uniprot/CO6A_CONER CO6A_CONER]] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 17:		Line 17:
	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 1g1z" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:47, 25 December 2014

OCA — Thu, 25 Dec 2014 06:47:54 GMT

←Older revision		Revision as of 06:47, 25 December 2014
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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CXD6A_CONER CXD6A_CONER]] Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 00:46, 23 December 2014

OCA — Tue, 23 Dec 2014 00:46:48 GMT

←Older revision		Revision as of 00:46, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z 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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z 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: Gall, F Le.]]	+	[[Category: Gall, F Le]]
-	[[Category: Lamthanh, H.]]	+	[[Category: Lamthanh, H]]
-	[[Category: Lancelin, J M.]]	+	[[Category: Lancelin, J M]]
-	[[Category: Menez, A.]]	+	[[Category: Menez, A]]
-	[[Category: Volpon, L.]]	+	[[Category: Volpon, L]]
	[[Category: Cis/trans isomerism of leu12-pro13 peptide bond]]		[[Category: Cis/trans isomerism of leu12-pro13 peptide bond]]
	[[Category: Hydroxyproline]]		[[Category: Hydroxyproline]]
	[[Category: Three disulfide linkage]]		[[Category: Three disulfide linkage]]
	[[Category: Toxin]]		[[Category: Toxin]]

OCA at 14:38, 28 September 2014

OCA — Sun, 28 Sep 2014 14:38:45 GMT

←Older revision		Revision as of 14:38, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1g1z.~~png~~\|~~left~~\|~~200px~~]]	+	==NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer==
		+	<StructureSection load='1g1z' size='340' side='right' caption='[[1g1z]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1Z FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1p\|1g1p]]</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=1g1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1z RCSB], [http://www.ebi.ac.uk/pdbsum/1g1z PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Delta-conotoxin EVIA, from Conus ermineus, is a 32-residue polypeptide cross-linked by three disulfide bonds forming a four-loop framework. delta-Conotoxin EVIA is the first conotoxin known to inhibit sodium channel inactivation in neuronal membranes from amphibians and mammals (subtypes rNa(v)1.2a, rNa(v)1.3, and rNa(v)1.6), without affecting rat skeletal muscle (subtype rNa(v)1.4) and human cardiac muscle (subtype hNa(v)1.5) sodium channel (Barbier, J., Lamthanh, H., Le Gall, F., Favreau, P., Benoit, E., Chen, H., Gilles, N., Ilan, N., Heinemann, S. F., Gordon, D., Menez, A., and Molgo, J. (2004) J. Biol. Chem. 279, 4680-4685). Its structure was solved by NMR and is characterized by a 1:1 cis/trans isomerism of the Leu(12)-Pro(13) peptide bond in slow exchange on the NMR time scale. The structure of both cis and trans isomers could be calculated separately. The isomerism occurs within a specific long disordered loop 2, including residues 11-19. These contribute to an important hydrophobic patch on the surface of the toxin. The rest of the structure matches the "inhibitor cystine-knot motif" of conotoxins from the "O superfamily" with a high structural order. To probe a possible functional role of the Leu(12)-Pro(13) cis/trans isomerism, a Pro(13) --> Ala delta-conotoxin EVIA was synthesized and shown to exist only as a trans isomer. P13A delta-conotoxin EVIA was estimated only two times less active than the wild-type EVIA in binding competition to rat brain synaptosomes and when injected intracerebroventricularly into mice.

-	~~{{STRUCTURE_1g1z\| PDB=1g1z \| SCENE= }}~~	+	NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels.,Volpon L, Lamthanh H, Barbier J, Gilles N, Molgo J, Menez A, Lancelin JM J Biol Chem. 2004 May 14;279(20):21356-66. Epub 2004 Feb 19. PMID:14976206<ref>PMID:14976206</ref>

-	~~===NMR Solution Structures~~ of ~~delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14976206}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[1g1z]] is a 1 chain structure. Full experimental information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA].~~	+	</StructureSection>
	[[Category: Gall, F Le.]]		[[Category: Gall, F Le.]]
	[[Category: Lamthanh, H.]]		[[Category: Lamthanh, H.]]

OCA: Protected "1g1z" [edit=sysop:move=sysop]

OCA — Wed, 21 Nov 2012 16:24:45 GMT

Protected "1g1z" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:24, 21 November 2012

OCA at 16:24, 21 November 2012

OCA — Wed, 21 Nov 2012 16:24:44 GMT

←Older revision		Revision as of 16:24, 21 November 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1g1z.png\|left\|200px]]		[[Image:1g1z.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1g1z", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1g1z\| PDB=1g1z \| SCENE= }}		{{STRUCTURE_1g1z\| PDB=1g1z \| SCENE= }}

	===NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer===		===NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels, LEU12-PRO13 Cis isomer===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14976206}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14976206 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14976206}}		{{ABSTRACT_PUBMED_14976206}}

	==About this Structure==		==About this Structure==
-	~~1G1Z is a~~ [[~~Single protein~~]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA].	+	[[1g1z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Z OCA].
-		+
-	~~==Reference==~~	+
-	NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels., Volpon L, Lamthanh H, Barbier J, Gilles N, Molgo J, Menez A, Lancelin JM, J Biol Chem. 2004 May 14;279(20):21356-66. Epub 2004 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14976206 14976206]	+
-	~~[[Category: Single protein]]~~	+
	[[Category: Gall, F Le.]]		[[Category: Gall, F Le.]]
	[[Category: Lamthanh, H.]]		[[Category: Lamthanh, H.]]
Line 33:		Line 17:
	[[Category: Hydroxyproline]]		[[Category: Hydroxyproline]]
	[[Category: Three disulfide linkage]]		[[Category: Three disulfide linkage]]
-		+	[[Category: Toxin]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Jul 1 04:17:08 2008''~~	+