4ni2 - Revision history

OCA at 16:57, 20 September 2023

2023-09-20T16:57:30Z

←Older revision		Revision as of 16:57, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NI2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [https://pdbe.org/4ni2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [https://pdbe.org/4ni2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:29, 11 January 2023

2023-01-11T08:29:31Z

←Older revision		Revision as of 08:29, 11 January 2023
Line 1:		Line 1:

	==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase==		==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase==
-	<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4ni2' size='340' side='right'caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NI2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NI2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [https://pdbe.org/4ni2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [~~http~~://pdbe.org/4ni2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN] Moyamoya disease with early-onset achalasia. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4ni2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ni2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Guanylate cyclase 3D structures\|Guanylate cyclase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Guanylate cyclase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Garcin~~, E D~~]]	+	[[Category: Garcin ED]]
-	[[Category: Seeger, F]]	+	[[Category: Seeger F]]
-	[[Category: Tainer~~, J A~~]]	+	[[Category: Tainer JA]]
-	[[Category: Williams~~, G J]]~~	+	[[Category: Williams GJ]]
-	~~[[Category: Cgmp biosynthesis]]~~	+
-	~~[[Category: Cyclase]]~~	+
-	~~[[Category: Cytosol]]~~	+
-	~~[[Category: Gtp-binding]]~~	+
-	~~[[Category: Heterodimeric]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Nitric oxide]]~~	+
-	~~[[Category: Nucleotide binding~~]]	+

OCA at 13:18, 11 August 2016

2016-08-11T13:18:00Z

←Older revision		Revision as of 13:18, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase==		==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase==
	<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([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">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([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/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ni2 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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [http://pdbe.org/4ni2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4ni2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:11, 5 January 2015

2015-01-05T09:11:03Z

←Older revision		Revision as of 09:11, 5 January 2015
Line 2:		Line 2:
	<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. <br>	+	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NI2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([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">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ni2 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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ni2 PDBsum]</span></td></tr>
-	<table>	+	</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 14:
	Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.,Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED Biochemistry. 2014 Apr 8;53(13):2153-65. doi: 10.1021/bi500129k. Epub 2014 Mar, 26. PMID:24669844<ref>PMID:24669844</ref>		Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.,Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED Biochemistry. 2014 Apr 8;53(13):2153-65. doi: 10.1021/bi500129k. Epub 2014 Mar, 26. PMID:24669844<ref>PMID:24669844</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 22:		Line 22:
	[[Category: Guanylate cyclase]]		[[Category: Guanylate cyclase]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Garcin, E D.]]	+	[[Category: Garcin, E D]]
-	[[Category: Seeger, F.]]	+	[[Category: Seeger, F]]
-	[[Category: Tainer, J A.]]	+	[[Category: Tainer, J A]]
-	[[Category: Williams, G J.]]	+	[[Category: Williams, G J]]
	[[Category: Cgmp biosynthesis]]		[[Category: Cgmp biosynthesis]]
	[[Category: Cyclase]]		[[Category: Cyclase]]

OCA at 06:44, 7 May 2014

2014-05-07T06:44:48Z

←Older revision		Revision as of 06:44, 7 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ni2\| PDB=4ni2 \| SCENE= }}~~	+	==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase==
-	===Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase===	+	<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24669844}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ni2]] 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=4NI2 OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUC1B3, GUCSB3, GUCY1B1, GUCY1B3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ni2 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Soluble guanylate cyclase (sGC) plays a central role in the cardiovascular system and is a drug target for the treatment of pulmonary hypertension. While the three-dimensional structure of sGC is unknown, studies suggest that binding of the regulatory domain to the catalytic domain maintains sGC in an autoinhibited basal state. The activation signal, binding of NO to heme, is thought to be transmitted via the regulatory and dimerization domains to the cyclase domain and unleashes the full catalytic potential of sGC. Consequently, isolated catalytic domains should show catalytic turnover comparable to that of activated sGC. Using X-ray crystallography, activity measurements, and native mass spectrometry, we show unambiguously that human isolated catalytic domains are much less active than basal sGC, while still forming heterodimers. We identified key structural elements regulating the dimer interface and propose a novel role for residues located in an interfacial flap and a hydrogen bond network as key modulators of the orientation of the catalytic subunits. We demonstrate that even in the absence of the regulatory domain, additional sGC domains are required to guide the appropriate conformation of the catalytic subunits associated with high activity. Our data support a novel regulatory mechanism whereby sGC activity is tuned by distinct domain interactions that either promote or inhibit catalytic activity. These results further our understanding of heterodimerization and activation of sGC and open additional drug discovery routes for targeting the NO-sGC-cGMP pathway via the design of small molecules that promote a productive conformation of the catalytic subunits or disrupt inhibitory domain interactions.

-	~~==About this Structure==~~	+	Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.,Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED Biochemistry. 2014 Apr 8;53(13):2153-65. doi: 10.1021/bi500129k. Epub 2014 Mar, 26. PMID:24669844<ref>PMID:24669844</ref>
-	~~[[4ni2]]~~ is ~~a 2 chain structure~~. ~~Full crystallographic information is available from [http~~:~~//oca~~.~~weizmann.ac~~.il/~~oca-bin/ocashort?id=4NI2 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024669844</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Guanylate cyclase]]		[[Category: Guanylate cyclase]]
		+	[[Category: Human]]
	[[Category: Garcin, E D.]]		[[Category: Garcin, E D.]]
	[[Category: Seeger, F.]]		[[Category: Seeger, F.]]

OCA at 09:37, 16 April 2014

2014-04-16T09:37:46Z

←Older revision		Revision as of 09:37, 16 April 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4ni2\| PDB=4ni2 \| SCENE= }}
		+	===Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase===
		+	{{ABSTRACT_PUBMED_24669844}}

-	~~The entry~~ 4ni2 is ~~ON HOLD~~	+	==About this Structure==
		+	[[4ni2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NI2 OCA].

-	~~Authors~~: Seeger, F.~~, Williams, G.J.,~~ Tainer, J.A., ~~Garcin, E.D~~.	+	==Reference==
-		+	<ref group="xtra">PMID:024669844</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Crystal structure of the heterodimeric catalytic domain of wild~~-~~type human soluble guanylate cyclase~~	+	[[Category: Guanylate cyclase]]
		+	[[Category: Garcin, E D.]]
		+	[[Category: Seeger, F.]]
		+	[[Category: Tainer, J A.]]
		+	[[Category: Williams, G J.]]
		+	[[Category: Cgmp biosynthesis]]
		+	[[Category: Cyclase]]
		+	[[Category: Cytosol]]
		+	[[Category: Gtp-binding]]
		+	[[Category: Heterodimeric]]
		+	[[Category: Lyase]]
		+	[[Category: Metal-binding]]
		+	[[Category: Nitric oxide]]
		+	[[Category: Nucleotide binding]]

OCA: Protected "4ni2" [edit=sysop:move=sysop]

2013-11-13T07:50:08Z

Protected "4ni2" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:50, 13 November 2013

OCA: New page: '''Unreleased structure''' The entry 4ni2 is ON HOLD Authors: Seeger, F., Williams, G.J., Tainer, J.A., Garcin, E.D. Description: Crystal structure of the heterodimeric catalytic domai...

2013-11-13T07:50:07Z

New page: '''Unreleased structure''' The entry 4ni2 is ON HOLD Authors: Seeger, F., Williams, G.J., Tainer, J.A., Garcin, E.D. Description: Crystal structure of the heterodimeric catalytic domai...

New page

'''Unreleased structure'''

The entry 4ni2 is ON HOLD

Authors: Seeger, F., Williams, G.J., Tainer, J.A., Garcin, E.D.

Description: Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase