1cod - Revision history

OCA at 08:22, 6 November 2024

2024-11-06T08:22:57Z

← Older revision		Revision as of 08:22, 6 November 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod ProSAT]</span></td></tr>
	</table>		</table>
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cod_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cod_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cod ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cod ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The solution conformation of cobrotoxin has been determined by using proton nuclear magnetic resonance spectroscopy. With the combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of cobrotoxin was completely assigned (Yu et al., 1990). A set of 435 approximate interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 29 dihedral angle constraints (from coupling constant measurements) and 26 hydrogen bonding restraints (from the pattern of short-range NOEs), form the basis of 3-D structure determination by the hybrid distance geometry-dynamical simulated annealing method. The 23 structures that were obtained satisfy the experimental restraints, display small deviation from idealized covalent geometry, and possess good nonbonded contacts. Analysis of converged structures indicated that there are two antiparallel beta sheets (double and triple stranded), duly confirming our earlier observations. These are well defined in terms of both atomic root mean square (RMS) differences and backbone torsional angles. The average backbone RMS deviation between the calculated structures and the mean structure, for the beta-sheet regions, is 0.92 A. The mean solution structure was compared with the X-ray crystal structure of erabutoxin b, the homologous protein. This yielded information that both structures resemble each other except at the exposed loop/surface regions, where the solution structure seems to possess more flexibility.

			Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.,Yu C, Bhaskaran R, Chuang LC, Yang CC Biochemistry. 1993 Mar 9;32(9):2131-6. PMID:8443154<ref>PMID:8443154</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 1cod" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:41, 13 March 2024

2024-03-13T15:41:09Z

← Older revision		Revision as of 15:41, 13 March 2024
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	==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==		==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==
	<StructureSection load='1cod' size='340' side='right'caption='[[1cod~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>		<StructureSection load='1cod' size='340' side='right'caption='[[1cod]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ansp_6988 Ansp 6988~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1coe\|1coe]]</div~~></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~3S1CB_NAJAT 3S1CB_NAJAT]~~] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. ~~Has a higher toxicity than cobrotoxin-b.~~		[https://www.uniprot.org/uniprot/3S1CB_NAJNA 3S1CB_NAJNA] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.[UniProtKB:P60775]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cod ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cod ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The solution conformation of cobrotoxin has been determined by using proton nuclear magnetic resonance spectroscopy. With the combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of cobrotoxin was completely assigned (Yu et al., 1990). A set of 435 approximate interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 29 dihedral angle constraints (from coupling constant measurements) and 26 hydrogen bonding restraints (from the pattern of short-range NOEs), form the basis of 3-D structure determination by the hybrid distance geometry-dynamical simulated annealing method. The 23 structures that were obtained satisfy the experimental restraints, display small deviation from idealized covalent geometry, and possess good nonbonded contacts. Analysis of converged structures indicated that there are two antiparallel beta sheets (double and triple stranded), duly confirming our earlier observations. These are well defined in terms of both atomic root mean square (RMS) differences and backbone torsional angles. The average backbone RMS deviation between the calculated structures and the mean structure, for the beta-sheet regions, is 0.92 A. The mean solution structure was compared with the X-ray crystal structure of erabutoxin b, the homologous protein. This yielded information that both structures resemble each other except at the exposed loop/surface regions, where the solution structure seems to possess more flexibility.

	Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.,Yu C, Bhaskaran R, Chuang LC, Yang CC Biochemistry. 1993 Mar 9;32(9):2131-6. PMID:8443154<ref>PMID:8443154</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1cod" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Ansp 6988]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Bhaskaran, R~~]]		[[Category: Naja atra]]
	[[Category: ~~Yang, C C~~]]		[[Category: Bhaskaran R]]
	[[Category: ~~Yu, C~~]]		[[Category: Yang CC]]
	[[Category: ~~Short neurotoxin~~]]		[[Category: Yu C]]

OCA at 10:33, 16 February 2022

2022-02-16T10:33:50Z

← Older revision		Revision as of 10:33, 16 February 2022
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	<StructureSection load='1cod' size='340' side='right'caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cod' size='340' side='right'caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ansp_6988 Ansp 6988]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1coe\|1coe]]</div></td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1coe\|1coe]]</div></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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Ansp 6988]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Bhaskaran, R]]		[[Category: Bhaskaran, R]]

OCA at 15:17, 3 March 2021

2021-03-03T15:17:56Z

← Older revision		Revision as of 15:17, 3 March 2021
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	<StructureSection load='1cod' size='340' side='right'caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cod' size='340' side='right'caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1coe\|1coe]]</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [~~http~~://pdbe.org/1cod PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1cod PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [https://pdbe.org/1cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [https://www.ebi.ac.uk/pdbsum/1cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/3S1CB_NAJAT 3S1CB_NAJAT]] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Has a higher toxicity than cobrotoxin-b.		[[https://www.uniprot.org/uniprot/3S1CB_NAJAT 3S1CB_NAJAT]] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Has a higher toxicity than cobrotoxin-b.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:17, 29 May 2019

2019-05-29T07:17:16Z

← Older revision		Revision as of 07:17, 29 May 2019
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	==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==		==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==
	<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cod' size='340' side='right'caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cod_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cod_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Bhaskaran, R]]		[[Category: Bhaskaran, R]]
	[[Category: Yang, C C]]		[[Category: Yang, C C]]
	[[Category: Yu, C]]		[[Category: Yu, C]]
	[[Category: Short neurotoxin]]		[[Category: Short neurotoxin]]

OCA at 11:23, 24 August 2017

2017-08-24T11:23:27Z

← Older revision		Revision as of 11:23, 24 August 2017
Line 1:		Line 1:

	==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==		==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==
	<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Chinese_cobra Chinese cobra]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://pdbe.org/1cod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://pdbe.org/1cod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cod ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Chinese cobra]]~~
	[[Category: Bhaskaran, R]]		[[Category: Bhaskaran, R]]
	[[Category: Yang, C C]]		[[Category: Yang, C C]]
	[[Category: Yu, C]]		[[Category: Yu, C]]
	[[Category: Short neurotoxin]]		[[Category: Short neurotoxin]]

OCA at 07:47, 11 September 2015

2015-09-11T07:47:56Z

← Older revision		Revision as of 07:47, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Naja_atra Naja atra~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_cobra Chinese cobra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://pdbe.org/1cod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/3S1CB_NAJAT 3S1CB_NAJAT]] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Has a higher toxicity than cobrotoxin-b.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	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 1cod" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Naja atra~~]]		[[Category: Chinese cobra]]
	[[Category: Bhaskaran, R]]		[[Category: Bhaskaran, R]]
	[[Category: Yang, C C]]		[[Category: Yang, C C]]
	[[Category: Yu, C]]		[[Category: Yu, C]]
	[[Category: Short neurotoxin]]		[[Category: Short neurotoxin]]

OCA at 22:06, 22 December 2014

2014-12-22T22:06:17Z

← Older revision		Revision as of 22:06, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod 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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Naja atra]]		[[Category: Naja atra]]
	[[Category: Bhaskaran, R.]]		[[Category: Bhaskaran, R]]
	[[Category: Yang, C C.]]		[[Category: Yang, C C]]
	[[Category: Yu, C.]]		[[Category: Yu, C]]
	[[Category: Short neurotoxin]]		[[Category: Short neurotoxin]]

OCA at 09:28, 27 August 2014

2014-08-27T09:28:30Z

← Older revision		Revision as of 09:28, 27 August 2014
Line 1:		Line 1:
	[[Image:~~1cod~~.~~png~~\|~~left~~\|~~200px~~]]		==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==
			<StructureSection load='1cod' size='340' side='right' caption='[[1cod]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COD FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1coe\|1coe]]</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=1cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cod RCSB], [http://www.ebi.ac.uk/pdbsum/1cod PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cod_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The solution conformation of cobrotoxin has been determined by using proton nuclear magnetic resonance spectroscopy. With the combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of cobrotoxin was completely assigned (Yu et al., 1990). A set of 435 approximate interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 29 dihedral angle constraints (from coupling constant measurements) and 26 hydrogen bonding restraints (from the pattern of short-range NOEs), form the basis of 3-D structure determination by the hybrid distance geometry-dynamical simulated annealing method. The 23 structures that were obtained satisfy the experimental restraints, display small deviation from idealized covalent geometry, and possess good nonbonded contacts. Analysis of converged structures indicated that there are two antiparallel beta sheets (double and triple stranded), duly confirming our earlier observations. These are well defined in terms of both atomic root mean square (RMS) differences and backbone torsional angles. The average backbone RMS deviation between the calculated structures and the mean structure, for the beta-sheet regions, is 0.92 A. The mean solution structure was compared with the X-ray crystal structure of erabutoxin b, the homologous protein. This yielded information that both structures resemble each other except at the exposed loop/surface regions, where the solution structure seems to possess more flexibility.

	~~{{STRUCTURE_1cod\| PDB=1cod \| SCENE= }}~~		Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.,Yu C, Bhaskaran R, Chuang LC, Yang CC Biochemistry. 1993 Mar 9;32(9):2131-6. PMID:8443154<ref>PMID:8443154</ref>

	~~===SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_8443154}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[1cod]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Naja_atra Naja atra]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1COD OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:008443154<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Naja atra]]		[[Category: Naja atra]]
	[[Category: Bhaskaran, R.]]		[[Category: Bhaskaran, R.]]

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

2012-10-21T20:25:30Z

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

← Older revision	Revision as of 20:25, 21 October 2012
(No difference)