1niw - Revision history

OCA at 08:50, 10 April 2024

OCA — Wed, 10 Apr 2024 08:50:21 GMT

←Older revision		Revision as of 08:50, 10 April 2024
Line 3:		Line 3:
	<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NIW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</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]] 2.05Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~MSE~~:~~SELENOMETHIONINE~~'>~~MSE~~</scene><~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [https://pdbe.org/1niw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [https://www.ebi.ac.uk/pdbsum/1niw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw 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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [https://pdbe.org/1niw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [https://www.ebi.ac.uk/pdbsum/1niw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw 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/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
	== 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=1niw 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=1niw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue peptide comprising the endothelial NOS (eNOS) CaM-binding region establishes their individual conformations and intermolecular interactions, and suggests the basis for isozyme-specific differences. The alpha-helical eNOS peptide binds in an antiparallel orientation to CaM through extensive hydrophobic interactions. Unique NOS interactions occur with: (i). the CaM flexible central linker, explaining its importance in NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific requirement for a bulky, hydrophobic residue at position 144. This binding mode expands mechanisms for CaM-mediated activation, explains eNOS deactivation by Thr495 phosphorylation, and implicates specific hydrophobic residues in the Ca(2+) independence of inducible NOS.
-
-	Structural basis for endothelial nitric oxide synthase binding to calmodulin.,Aoyagi M, Arvai AS, Tainer JA, Getzoff ED EMBO J. 2003 Feb 17;22(4):766-75. PMID:12574113<ref>PMID:12574113</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1niw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Aoyagi, M~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Arvai, A S~~]]	+	[[Category: Aoyagi M]]
-	[[Category: ~~Getzoff, E D~~]]	+	[[Category: Arvai AS]]
-	[[Category: ~~Tainer, J A~~]]	+	[[Category: Getzoff ED]]
-	[[Category: ~~Calcium-binding protein]]~~	+	[[Category: Tainer JA]]
-	~~[[Category: Nitric oxide]]~~	+
-	~~[[Category: No]]~~	+
-	~~[[Category: Signaling protein-oxidoreductase complex~~]]	+

OCA at 07:03, 25 August 2021

OCA — Wed, 25 Aug 2021 07:03:25 GMT

←Older revision		Revision as of 07:03, 25 August 2021
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	<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1NIW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [~~http~~://pdbe.org/1niw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1niw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw 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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [https://pdbe.org/1niw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [https://www.ebi.ac.uk/pdbsum/1niw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw 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]]

OCA at 18:25, 20 November 2019

OCA — Wed, 20 Nov 2019 18:25:17 GMT

←Older revision		Revision as of 18:25, 20 November 2019
Line 1:		Line 1:

	==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==		==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==
-	<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>	+	<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1niw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1niw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Aoyagi, M]]		[[Category: Aoyagi, M]]
	[[Category: Arvai, A S]]		[[Category: Arvai, A S]]

OCA at 07:13, 7 February 2018

OCA — Wed, 07 Feb 2018 07:13:08 GMT

←Older revision		Revision as of 07:13, 7 February 2018
Line 1:		Line 1:
		+
	==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==		==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==
	<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://pdbe.org/1niw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw 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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://pdbe.org/1niw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ni/1niw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ni/1niw_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 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1niw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1niw" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Calmodulin\|Calmodulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:06, 9 February 2016

OCA — Tue, 09 Feb 2016 22:06:58 GMT

←Older revision		Revision as of 22:06, 9 February 2016
Line 18:		Line 18:
	<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=1niw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:29, 11 September 2015

OCA — Fri, 11 Sep 2015 02:29:14 GMT

←Older revision		Revision as of 02:29, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw 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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://pdbe.org/1niw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1niw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Nitric-oxide synthase]]~~	+	[[Category: Buffalo rat]]
-	~~[[Category: Rattus norvegicus~~]]	+
	[[Category: Aoyagi, M]]		[[Category: Aoyagi, M]]
	[[Category: Arvai, A S]]		[[Category: Arvai, A S]]

OCA at 09:51, 25 December 2014

OCA — Thu, 25 Dec 2014 09:51:25 GMT

←Older revision		Revision as of 09:51, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw 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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw 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 35:		Line 37:
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Aoyagi, M.]]	+	[[Category: Aoyagi, M]]
-	[[Category: Arvai, A S.]]	+	[[Category: Arvai, A S]]
-	[[Category: Getzoff, E D.]]	+	[[Category: Getzoff, E D]]
-	[[Category: Tainer, J A.]]	+	[[Category: Tainer, J A]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Nitric oxide]]		[[Category: Nitric oxide]]
	[[Category: No]]		[[Category: No]]
	[[Category: Signaling protein-oxidoreductase complex]]		[[Category: Signaling protein-oxidoreductase complex]]

OCA at 16:01, 28 September 2014

OCA — Sun, 28 Sep 2014 16:01:28 GMT

←Older revision		Revision as of 16:01, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1niw.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==
		+	<StructureSection load='1niw' size='340' side='right' caption='[[1niw]], [[Resolution\|resolution]] 2.05Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [http://www.ebi.ac.uk/pdbsum/1niw 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/ni/1niw_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 enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue peptide comprising the endothelial NOS (eNOS) CaM-binding region establishes their individual conformations and intermolecular interactions, and suggests the basis for isozyme-specific differences. The alpha-helical eNOS peptide binds in an antiparallel orientation to CaM through extensive hydrophobic interactions. Unique NOS interactions occur with: (i). the CaM flexible central linker, explaining its importance in NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific requirement for a bulky, hydrophobic residue at position 144. This binding mode expands mechanisms for CaM-mediated activation, explains eNOS deactivation by Thr495 phosphorylation, and implicates specific hydrophobic residues in the Ca(2+) independence of inducible NOS.

-	~~{{STRUCTURE_1niw\| PDB=1niw \| SCENE= }}~~	+	Structural basis for endothelial nitric oxide synthase binding to calmodulin.,Aoyagi M, Arvai AS, Tainer JA, Getzoff ED EMBO J. 2003 Feb 17;22(4):766-75. PMID:12574113<ref>PMID:12574113</ref>

-	~~===Crystal structure~~ of ~~endothelial nitric oxide synthase peptide bound to calmodulin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12574113}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1niw]] is a 8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].~~	+

	==See Also==		==See Also==
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012574113<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]

OCA at 15:18, 20 October 2012

OCA — Sat, 20 Oct 2012 15:18:12 GMT

←Older revision		Revision as of 15:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1niw]] is a 8 chain structure ~~of [[Calmodulin]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].	+	[[1niw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].

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

OCA at 17:57, 26 July 2012

OCA — Thu, 26 Jul 2012 17:57:08 GMT

←Older revision		Revision as of 17:57, 26 July 2012
Line 1:		Line 1:
	[[Image:1niw.png\|left\|200px]]		[[Image:1niw.png\|left\|200px]]

-	<!--
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-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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	{{STRUCTURE_1niw\| PDB=1niw \| SCENE= }}		{{STRUCTURE_1niw\| PDB=1niw \| SCENE= }}

	===Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin===		===Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12574113}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12574113 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_12574113}}		{{ABSTRACT_PUBMED_12574113}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Calmodulin]]	+	*[[Calmodulin\|Calmodulin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12574113~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012574113</ref><references group="xtra"/>
	[[Category: Nitric-oxide synthase]]		[[Category: Nitric-oxide synthase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 35:		Line 24:
	[[Category: Nitric oxide]]		[[Category: Nitric oxide]]
	[[Category: No]]		[[Category: No]]
-	[[Category: Signaling protein/oxidoreductase complex]]	+	[[Category: Signaling protein-oxidoreductase complex]]