3eah - Revision history

OCA at 09:46, 21 February 2024

OCA — Wed, 21 Feb 2024 09:46:13 GMT

←Older revision		Revision as of 09:46, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3eah' size='340' side='right'caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3eah' size='340' side='right'caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.44Å</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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[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=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [https://pdbe.org/3eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [https://www.ebi.ac.uk/pdbsum/3eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah 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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [https://pdbe.org/3eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [https://www.ebi.ac.uk/pdbsum/3eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN]] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref> Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</ref>	+	[https://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref> Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</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=3eah 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=3eah 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 3eah" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[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 11:44, 16 February 2022

OCA — Wed, 16 Feb 2022 11:44:51 GMT

←Older revision		Revision as of 11:44, 16 February 2022
Line 1:		Line 1:

	==Structure of inhibited human eNOS oxygenase domain==		==Structure of inhibited human eNOS oxygenase domain==
-	<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>	+	<StructureSection load='3eah' size='340' side='right'caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EAH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [~~http~~://pdbe.org/3eah PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3eah PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah 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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [https://pdbe.org/3eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [https://www.ebi.ac.uk/pdbsum/3eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN]] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref> Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</ref>	+	[[https://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN]] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref> Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</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/>
Line 39:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Aberg, A]]		[[Category: Aberg, A]]
	[[Category: Andersson, G]]		[[Category: Andersson, G]]

OCA at 21:31, 2 December 2018

OCA — Sun, 02 Dec 2018 21:31:48 GMT

←Older revision		Revision as of 21:31, 2 December 2018
Line 1:		Line 1:
		+
	==Structure of inhibited human eNOS oxygenase domain==		==Structure of inhibited human eNOS oxygenase domain==
	<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://pdbe.org/3eah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah 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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://pdbe.org/3eah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3eah_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3eah_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 69:		Line 70:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Oxidoreductase calmodulin-binding]]		[[Category: Oxidoreductase calmodulin-binding]]
		+	[[Category: Polymorphism]]
	[[Category: Tetrahydrobiopterin]]		[[Category: Tetrahydrobiopterin]]
		+	[[Category: Zinc]]

OCA at 07:36, 10 February 2016

OCA — Wed, 10 Feb 2016 07:36:53 GMT

←Older revision		Revision as of 07:36, 10 February 2016
Line 2:		Line 2:
	<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah 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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://pdbe.org/3eah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	<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=3eah ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 3eah" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens]]~~	+	[[Category: Human]]
-	~~[[Category: Nitric-oxide synthase~~]]	+
	[[Category: Aberg, A]]		[[Category: Aberg, A]]
	[[Category: Andersson, G]]		[[Category: Andersson, G]]

OCA at 12:46, 25 December 2014

OCA — Thu, 25 Dec 2014 12:46:12 GMT

←Older revision		Revision as of 12:46, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAH FirstGlance]. <br>		<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah 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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN]] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref> Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[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 12:52, 29 September 2014

OCA — Mon, 29 Sep 2014 12:52:47 GMT

←Older revision		Revision as of 12:52, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3eah.~~png~~\|~~left~~\|200px]]	+	==Structure of inhibited human eNOS oxygenase domain==
		+	<StructureSection load='3eah' size='340' side='right' caption='[[3eah]], [[Resolution\|resolution]] 2.44Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]], [[3eai\|3eai]], [[3ebd\|3ebd]], [[3ebf\|3ebf]], [[3ej8\|3ej8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Nos3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [http://www.ebi.ac.uk/pdbsum/3eah 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/ea/3eah_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_3eah\| PDB=3eah \| 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 human eNOS oxygenase domain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18849972}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3eah]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH 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: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]

OCA at 16:50, 20 October 2012

OCA — Sat, 20 Oct 2012 16:50:09 GMT

←Older revision		Revision as of 16:50, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3eah]] is a 2 chain structure ~~of [[Nitric Oxide Synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].	+	[[3eah]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].

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

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

OCA — Thu, 26 Jul 2012 22:58:31 GMT

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

←Older revision

Revision as of 22:58, 26 July 2012

OCA at 22:58, 26 July 2012

OCA — Thu, 26 Jul 2012 22:58:29 GMT

←Older revision		Revision as of 22:58, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3eah.png\|left\|200px]]		[[Image:3eah.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3eah", 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_3eah\| PDB=3eah \| SCENE= }}		{{STRUCTURE_3eah\| PDB=3eah \| SCENE= }}

	===Structure of inhibited human eNOS oxygenase domain===		===Structure of inhibited human eNOS 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==
-	~~3EAH~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].	+	[[3eah]] is a 2 chain structure of [[Nitric Oxide Synthase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH 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: Homo sapiens]]		[[Category: Homo sapiens]]
	[[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 Tue Feb 17 16:33:07 2009''

OCA at 14:33, 17 February 2009

OCA — Tue, 17 Feb 2009 14:33:09 GMT

←Older revision		Revision as of 14:33, 17 February 2009
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	==About this Structure==		==About this Structure==
-	3EAH is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].	+	3EAH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].

	==Reference==		==Reference==
-	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:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18849972 18849972]~~	+	<ref group="xtra">PMID:18849972</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
-	[[Category: ~~Single protein~~]]	+	[[Category: Aberg, A.]]
-	[[Category: ~~Pdbx_ordinal=~~, ~~<PDBx~~:~~audit_author~~.]]	+	[[Category: Andersson, G.]]
		+	[[Category: Andrews, G.]]
		+	[[Category: Arvai, A S.]]
		+	[[Category: Cheshire, D R.]]
		+	[[Category: Connolly, S.]]
		+	[[Category: Crane, B R.]]
		+	[[Category: Garcin, E D.]]
		+	[[Category: Gensmantel, N P.]]
		+	[[Category: Getzoff, E D.]]
		+	[[Category: Hamley, P J.]]
		+	[[Category: Kroeger, M D.]]
		+	[[Category: Mallinder, P R.]]
		+	[[Category: Mete, A.]]
		+	[[Category: Nicholls, D J.]]
		+	[[Category: Rosenfeld, R J.]]
		+	[[Category: St-Gallay, S A.]]
		+	[[Category: Stuehr, D J.]]
		+	[[Category: Tainer, J A.]]
		+	[[Category: Tinker, A C.]]
		+	[[Category: Wallace, A V.]]
	[[Category: Fad]]		[[Category: Fad]]
	[[Category: Fmn]]		[[Category: Fmn]]
Line 42:		Line 61:
	[[Category: Zinc]]		[[Category: Zinc]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 14 20~~:24:06 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:33:07 2009''