3ebd - Revision history

OCA at 09:12, 13 August 2026

2026-08-13T09:12:02Z

← Older revision		Revision as of 09:12, 13 August 2026
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/3ebd_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/3ebd_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=3ebd 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=3ebd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Nitric oxide synthase (NOS) enzymes synthesize nitric oxide, a signal for vasodilatation and neurotransmission at low concentrations and a defensive cytotoxin at higher concentrations. The high active site conservation among all three NOS isozymes hinders the design of selective NOS inhibitors to treat inflammation, arthritis, stroke, septic shock and cancer. Our crystal structures and mutagenesis results identified an isozyme-specific induced-fit binding mode linking a cascade of conformational changes to a new specificity pocket. Plasticity of an isozyme-specific triad of distant second- and third-shell residues modulates conformational changes of invariant first-shell residues to determine inhibitor selectivity. To design potent and selective NOS inhibitors, we developed the anchored plasticity approach: anchor an inhibitor core in a conserved binding pocket, then extend rigid bulky substituents toward remote specificity pockets, which become accessible upon conformational changes of flexible residues. This approach exemplifies general principles for the design of selective enzyme inhibitors that overcome strong active site conservation.

			Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.,Garcin ED, Arvai AS, Rosenfeld RJ, Kroeger MD, Crane BR, Andersson G, Andrews G, Hamley PJ, Mallinder PR, Nicholls DJ, St-Gallay SA, Tinker AC, Gensmantel NP, Mete A, Cheshire DR, Connolly S, Stuehr DJ, Aberg A, Wallace AV, Tainer JA, Getzoff ED Nat Chem Biol. 2008 Nov;4(11):700-7. Epub 2008 Oct 12. PMID:18849972<ref>PMID:18849972</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 3ebd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 09:46, 21 February 2024

2024-02-21T09:46:35Z

← Older revision		Revision as of 09:46, 21 February 2024
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	<StructureSection load='3ebd' size='340' side='right'caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3ebd' size='340' side='right'caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EBD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EBD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.4Å</td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</div></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [https://pdbe.org/3ebd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [https://www.ebi.ac.uk/pdbsum/3ebd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebd 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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [https://pdbe.org/3ebd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [https://www.ebi.ac.uk/pdbsum/3ebd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>		[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 20:
	</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=3ebd 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=3ebd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Nitric oxide synthase (NOS) enzymes synthesize nitric oxide, a signal for vasodilatation and neurotransmission at low concentrations and a defensive cytotoxin at higher concentrations. The high active site conservation among all three NOS isozymes hinders the design of selective NOS inhibitors to treat inflammation, arthritis, stroke, septic shock and cancer. Our crystal structures and mutagenesis results identified an isozyme-specific induced-fit binding mode linking a cascade of conformational changes to a new specificity pocket. Plasticity of an isozyme-specific triad of distant second- and third-shell residues modulates conformational changes of invariant first-shell residues to determine inhibitor selectivity. To design potent and selective NOS inhibitors, we developed the anchored plasticity approach: anchor an inhibitor core in a conserved binding pocket, then extend rigid bulky substituents toward remote specificity pockets, which become accessible upon conformational changes of flexible residues. This approach exemplifies general principles for the design of selective enzyme inhibitors that overcome strong active site conservation.

	Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.,Garcin ED, Arvai AS, Rosenfeld RJ, Kroeger MD, Crane BR, Andersson G, Andrews G, Hamley PJ, Mallinder PR, Nicholls DJ, St-Gallay SA, Tinker AC, Gensmantel NP, Mete A, Cheshire DR, Connolly S, Stuehr DJ, Aberg A, Wallace AV, Tainer JA, Getzoff ED Nat Chem Biol. 2008 Nov;4(11):700-7. Epub 2008 Oct 12. PMID:18849972<ref>PMID:18849972</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3ebd" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
Line 39:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Aberg, A]]		[[Category: Aberg A]]
	[[Category: Andersson, G]]		[[Category: Andersson G]]
	[[Category: Andrews, G]]		[[Category: Andrews G]]
	[[Category: Arvai~~, A S~~]]		[[Category: Arvai AS]]
	[[Category: Cheshire~~, D R~~]]		[[Category: Cheshire DR]]
	[[Category: Connolly, S]]		[[Category: Connolly S]]
	[[Category: Crane~~, B R~~]]		[[Category: Crane BR]]
	[[Category: Garcin~~, E D~~]]		[[Category: Garcin ED]]
	[[Category: Gensmantel~~, N P~~]]		[[Category: Gensmantel NP]]
	[[Category: Getzoff~~, E D~~]]		[[Category: Getzoff ED]]
	[[Category: Hamley~~, P J~~]]		[[Category: Hamley PJ]]
	[[Category: Kroeger~~, M D~~]]		[[Category: Kroeger MD]]
	[[Category: Mallinder~~, P R~~]]		[[Category: Mallinder PR]]
	[[Category: Mete, A]]		[[Category: Mete A]]
	[[Category: Nicholls~~, D J~~]]		[[Category: Nicholls DJ]]
	[[Category: Rosenfeld~~, R J~~]]		[[Category: Rosenfeld RJ]]
	[[Category: St-Gallay~~, S A~~]]		[[Category: St-Gallay SA]]
	[[Category: Stuehr~~, D J~~]]		[[Category: Stuehr DJ]]
	[[Category: Tainer~~, J A~~]]		[[Category: Tainer JA]]
	[[Category: Tinker~~, A C~~]]		[[Category: Tinker AC]]
	[[Category: Wallace~~, A V]]~~		[[Category: Wallace AV]]
	~~[[Category: Fad]]~~
	~~[[Category: Fmn]]~~
	~~[[Category: Heme]]~~
	~~[[Category: Iron]]~~
	~~[[Category: Metal-binding]]~~
	~~[[Category: Nadp]]~~
	~~[[Category: Nitric oxide synthase]]~~
	~~[[Category: No]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Oxidoreductase calmodulin-binding]]~~
	~~[[Category: Polymorphism]]~~
	~~[[Category: Tetrahydrobiopterin]]~~
	~~[[Category: Zinc~~]]

OCA at 11:45, 16 February 2022

2022-02-16T11:45:37Z

← Older revision		Revision as of 11:45, 16 February 2022
Line 1:		Line 1:

	==Structure of inhibited murine iNOS oxygenase domain==		==Structure of inhibited murine iNOS oxygenase domain==
	<StructureSection load='3ebd' size='340' side='right' caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3ebd' size='340' side='right'caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EBD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EBD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [~~http~~://pdbe.org/3ebd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ebd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebd 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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [https://pdbe.org/3ebd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [https://www.ebi.ac.uk/pdbsum/3ebd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>		[[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
	*[[Nitric Oxide Synthase\|Nitric Oxide Synthase]]		*[[Nitric Oxide Synthase 3D structures\|Nitric Oxide Synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Aberg, A]]		[[Category: Aberg, A]]

OCA at 21:22, 2 December 2018

2018-12-02T21:22:12Z

← Older revision		Revision as of 21:22, 2 December 2018
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/3ebd_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/3ebd_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 70:		Line 70:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Oxidoreductase calmodulin-binding]]		[[Category: Oxidoreductase calmodulin-binding]]
			[[Category: Polymorphism]]
	[[Category: Tetrahydrobiopterin]]		[[Category: Tetrahydrobiopterin]]
			[[Category: Zinc]]

OCA at 19:35, 5 August 2016

2016-08-05T19:35:45Z

← Older revision		Revision as of 19:35, 5 August 2016
Line 1:		Line 1:

	==Structure of inhibited murine iNOS oxygenase domain==		==Structure of inhibited murine iNOS oxygenase domain==
	<StructureSection load='3ebd' size='340' side='right' caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3ebd' size='340' side='right' caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EBD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EBD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-~~oxide_synthase~~ Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [http://www.ebi.ac.uk/pdbsum/3ebd 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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [http://pdbe.org/3ebd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [http://www.ebi.ac.uk/pdbsum/3ebd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=3ebd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3ebd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus]]~~		[[Category: Lk3 transgenic mice]]
	~~[[Category: Nitric-oxide synthase~~]]
	[[Category: Aberg, A]]		[[Category: Aberg, A]]
	[[Category: Andersson, G]]		[[Category: Andersson, G]]

OCA at 21:21, 25 December 2014

2014-12-25T21:21:04Z

← Older revision		Revision as of 21:21, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EBD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EBD FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [http://www.ebi.ac.uk/pdbsum/3ebd 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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [http://www.ebi.ac.uk/pdbsum/3ebd PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
	[[Category: Aberg, A.]]		[[Category: Aberg, A]]
	[[Category: Andersson, G.]]		[[Category: Andersson, G]]
	[[Category: Andrews, G.]]		[[Category: Andrews, G]]
	[[Category: Arvai, A S.]]		[[Category: Arvai, A S]]
	[[Category: Cheshire, D R.]]		[[Category: Cheshire, D R]]
	[[Category: Connolly, S.]]		[[Category: Connolly, S]]
	[[Category: Crane, B R.]]		[[Category: Crane, B R]]
	[[Category: Garcin, E D.]]		[[Category: Garcin, E D]]
	[[Category: Gensmantel, N P.]]		[[Category: Gensmantel, N P]]
	[[Category: Getzoff, E D.]]		[[Category: Getzoff, E D]]
	[[Category: Hamley, P J.]]		[[Category: Hamley, P J]]
	[[Category: Kroeger, M D.]]		[[Category: Kroeger, M D]]
	[[Category: Mallinder, P R.]]		[[Category: Mallinder, P R]]
	[[Category: Mete, A.]]		[[Category: Mete, A]]
	[[Category: Nicholls, D J.]]		[[Category: Nicholls, D J]]
	[[Category: Rosenfeld, R J.]]		[[Category: Rosenfeld, R J]]
	[[Category: St-Gallay, S A.]]		[[Category: St-Gallay, S A]]
	[[Category: Stuehr, D J.]]		[[Category: Stuehr, D J]]
	[[Category: Tainer, J A.]]		[[Category: Tainer, J A]]
	[[Category: Tinker, A C.]]		[[Category: Tinker, A C]]
	[[Category: Wallace, A V.]]		[[Category: Wallace, A V]]
	[[Category: Fad]]		[[Category: Fad]]
	[[Category: Fmn]]		[[Category: Fmn]]

OCA at 11:25, 29 September 2014

2014-09-29T11:25:39Z

← Older revision		Revision as of 11:25, 29 September 2014
Line 1:		Line 1:
	[[Image:~~3ebd~~.~~png~~\|~~left~~\|~~200px~~]]		==Structure of inhibited murine iNOS oxygenase domain==
			<StructureSection load='3ebd' size='340' side='right' caption='[[3ebd]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EBD FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=329:(2S)-2-METHYL-2,3-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5-AMINE'>329</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e65\|3e65]], [[3e67\|3e67]], [[3e68\|3e68]], [[3e6l\|3e6l]], [[3e6n\|3e6n]], [[3e6o\|3e6o]], [[3e6t\|3e6t]], [[3e7g\|3e7g]], [[3e7i\|3e7i]], [[3e7m\|3e7m]], [[3e7s\|3e7s]], [[3e7t\|3e7t]], [[3eah\|3eah]], [[3eai\|3eai]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos2, Inosl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></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=3ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ebd RCSB], [http://www.ebi.ac.uk/pdbsum/3ebd 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/eb/3ebd_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 ==
			Nitric oxide synthase (NOS) enzymes synthesize nitric oxide, a signal for vasodilatation and neurotransmission at low concentrations and a defensive cytotoxin at higher concentrations. The high active site conservation among all three NOS isozymes hinders the design of selective NOS inhibitors to treat inflammation, arthritis, stroke, septic shock and cancer. Our crystal structures and mutagenesis results identified an isozyme-specific induced-fit binding mode linking a cascade of conformational changes to a new specificity pocket. Plasticity of an isozyme-specific triad of distant second- and third-shell residues modulates conformational changes of invariant first-shell residues to determine inhibitor selectivity. To design potent and selective NOS inhibitors, we developed the anchored plasticity approach: anchor an inhibitor core in a conserved binding pocket, then extend rigid bulky substituents toward remote specificity pockets, which become accessible upon conformational changes of flexible residues. This approach exemplifies general principles for the design of selective enzyme inhibitors that overcome strong active site conservation.

	~~{{STRUCTURE_3ebd\| PDB=3ebd \| SCENE= }}~~		Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.,Garcin ED, Arvai AS, Rosenfeld RJ, Kroeger MD, Crane BR, Andersson G, Andrews G, Hamley PJ, Mallinder PR, Nicholls DJ, St-Gallay SA, Tinker AC, Gensmantel NP, Mete A, Cheshire DR, Connolly S, Stuehr DJ, Aberg A, Wallace AV, Tainer JA, Getzoff ED Nat Chem Biol. 2008 Nov;4(11):700-7. Epub 2008 Oct 12. PMID:18849972<ref>PMID:18849972</ref>

	~~===Structure~~ of ~~inhibited murine iNOS oxygenase domain===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_18849972}}~~

	~~==About this Structure==~~
	~~[[3ebd]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus]~~. ~~Full crystallographic information is available from [http://oca.weizmann.ac.il~~/~~oca-bin/ocashort?id=3EBD OCA].~~

	==See Also==		==See Also==
	*[[Nitric Oxide Synthase\|Nitric Oxide Synthase]]		*[[Nitric Oxide Synthase\|Nitric Oxide Synthase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:018849972<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]

OCA at 21:48, 20 October 2012

2012-10-20T21:48:14Z

← Older revision		Revision as of 21:48, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3ebd]] is a 2 chain structure ~~of [[Nitric Oxide Synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA].		[[3ebd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA].

	==See Also==		==See Also==

OCA: Protected "3ebd" [edit=sysop:move=sysop]

2012-07-27T14:20:24Z

Protected "3ebd" [edit=sysop:move=sysop]

← Older revision	Revision as of 14:20, 27 July 2012
(No difference)

OCA at 14:20, 27 July 2012

2012-07-27T14:20:22Z

← Older revision		Revision as of 14:20, 27 July 2012
Line 1:		Line 1:
	~~{{Seed}}~~
	[[Image:3ebd.png\|left\|200px]]		[[Image:3ebd.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3ebd", 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_3ebd\| PDB=3ebd \| SCENE= }}		{{STRUCTURE_3ebd\| PDB=3ebd \| SCENE= }}

	===Structure of inhibited murine iNOS oxygenase domain===		===Structure of inhibited murine iNOS oxygenase domain===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_18849972}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 18849972 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_18849972}}		{{ABSTRACT_PUBMED_18849972}}

	==About this Structure==		==About this Structure==
	~~3EBD~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA].		[[3ebd]] is a 2 chain structure of [[Nitric Oxide Synthase]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBD OCA].

			==See Also==
			*[[Nitric Oxide Synthase\|Nitric Oxide Synthase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~18849972~~</ref><references group="xtra"/>		<ref group="xtra">PMID:018849972</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
Line 57:		Line 48:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Oxidoreductase calmodulin-binding]]		[[Category: Oxidoreductase calmodulin-binding]]
	~~[[Category: Polymorphism]]~~
	[[Category: Tetrahydrobiopterin]]		[[Category: Tetrahydrobiopterin]]
	~~[[Category: Zinc]]~~

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:58:12 2009''~~