5c6c - Revision history

OCA at 12:19, 6 March 2024

2024-03-06T12:19:04Z

←Older revision		Revision as of 12:19, 6 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5c6c]] 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=5C6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6C FirstGlance]. <br>		<table><tr><td colspan='2'>[[5c6c]] 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=5C6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6C 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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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='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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [https://pdbe.org/5c6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [https://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c 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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [https://pdbe.org/5c6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [https://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/KGP2_HUMAN KGP2_HUMAN]		[https://www.uniprot.org/uniprot/KGP2_HUMAN KGP2_HUMAN]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Membrane-bound cGMP-dependent protein kinase (PKG) II is a key regulator of bone growth, renin secretion, and memory formation. Despite its crucial physiological roles, little is known about its cyclic nucleotide selectivity mechanism due to a lack of structural information. Here, we find that the C-terminal cyclic nucleotide binding (CNB-B) domain of PKG II binds cGMP with higher affinity and selectivity, compared to its N-terminal CNB (CNB-A) domain. To understand the structural basis of cGMP selectivity, we solved co-crystal structures of the CNB domains with cyclic nucleotides. Our structures combined with mutagenesis demonstrate that the guanine specific contacts at D412 and R415 of the alphaC-helix of CNB-B are crucial for cGMP selectivity and activation of PKG II. Structural comparison with the cGMP selective CNB domains of human PKG I and Plasmodium falciparum PKG (PfPKG) shows different contacts with the guanine moiety, revealing a unique cGMP selectivity mechanism for PKG II.
-
-	Structural Basis of Cyclic Nucleotide Selectivity in cGMP-Dependent Protein Kinase II.,Campbell JC, Kim JJ, Li KY, Huang GY, Reger AS, Matsuda S, Sankaran B, Link TM, Yuasa K, Ladbury JE, Casteel DE, Kim C J Biol Chem. 2016 Jan 14. pii: jbc.M115.691303. PMID:26769964<ref>PMID:26769964</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5c6c" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:21, 7 June 2023

2023-06-07T06:21:38Z

←Older revision		Revision as of 06:21, 7 June 2023
Line 3:		Line 3:
	<StructureSection load='5c6c' size='340' side='right'caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='5c6c' size='340' side='right'caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5c6c]] 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=5C6C OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5C6C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5c6c]] 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=5C6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6C 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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRKG2, PRKGR2 ([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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [https://pdbe.org/5c6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [https://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c 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/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [~~http~~://pdbe.org/5c6c PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/KGP2_HUMAN KGP2_HUMAN]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Transferase]]~~	+	[[Category: Campbell JC]]
-	[[Category: Campbell~~, J C~~]]	+	[[Category: Huang GY]]
-	[[Category: Huang~~, G Y~~]]	+	[[Category: Kim CW]]
-	[[Category: Kim~~, C W~~]]	+	[[Category: Kim JJ]]
-	[[Category: Kim~~, J J~~]]	+	[[Category: Reger AS]]
-	[[Category: Reger~~, A S~~]]	+	[[Category: Sankaran B]]
-	[[Category: Sankaran, B]]	+
-	~~[[Category: Binding site]]~~	+
-	~~[[Category: Cyclic amp]]~~	+
-	~~[[Category: Cyclic gmp]]~~	+
-	~~[[Category: Cyclic gmp-dependent protein kinase type ii]]~~	+
-	~~[[Category: Mutagenesis]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Site-directed~~]]	+

OCA at 11:10, 25 December 2019

2019-12-25T11:10:31Z

←Older revision		Revision as of 11:10, 25 December 2019
Line 1:		Line 1:

	==PKG II's Amino Terminal Cyclic Nucleotide Binding Domain (CNB-A) in a complex with cAMP==		==PKG II's Amino Terminal Cyclic Nucleotide Binding Domain (CNB-A) in a complex with cAMP==
-	<StructureSection load='5c6c' size='340' side='right' caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>	+	<StructureSection load='5c6c' size='340' side='right'caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5c6c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5c6c]] 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=5C6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6C 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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRKG2, PRKGR2 ([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/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c ProSAT]</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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c ProSAT]</span></td></tr>
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Campbell, J C]]		[[Category: Campbell, J C]]

OCA at 04:35, 21 September 2017

2017-09-21T04:35:46Z

←Older revision		Revision as of 04:35, 21 September 2017
Line 6:		Line 6:
	</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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c 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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6c ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 16:50, 10 May 2016

2016-05-10T16:50:34Z

←Older revision		Revision as of 16:50, 10 May 2016
Line 1:		Line 1:
		+
	==PKG II's Amino Terminal Cyclic Nucleotide Binding Domain (CNB-A) in a complex with cAMP==		==PKG II's Amino Terminal Cyclic Nucleotide Binding Domain (CNB-A) in a complex with cAMP==
	<StructureSection load='5c6c' size='340' side='right' caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='5c6c' size='340' side='right' caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>
Line 7:		Line 8:
	<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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c 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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Membrane-bound cGMP-dependent protein kinase (PKG) II is a key regulator of bone growth, renin secretion, and memory formation. Despite its crucial physiological roles, little is known about its cyclic nucleotide selectivity mechanism due to a lack of structural information. Here, we find that the C-terminal cyclic nucleotide binding (CNB-B) domain of PKG II binds cGMP with higher affinity and selectivity, compared to its N-terminal CNB (CNB-A) domain. To understand the structural basis of cGMP selectivity, we solved co-crystal structures of the CNB domains with cyclic nucleotides. Our structures combined with mutagenesis demonstrate that the guanine specific contacts at D412 and R415 of the alphaC-helix of CNB-B are crucial for cGMP selectivity and activation of PKG II. Structural comparison with the cGMP selective CNB domains of human PKG I and Plasmodium falciparum PKG (PfPKG) shows different contacts with the guanine moiety, revealing a unique cGMP selectivity mechanism for PKG II.
		+
		+	Structural Basis of Cyclic Nucleotide Selectivity in cGMP-Dependent Protein Kinase II.,Campbell JC, Kim JJ, Li KY, Huang GY, Reger AS, Matsuda S, Sankaran B, Link TM, Yuasa K, Ladbury JE, Casteel DE, Kim C J Biol Chem. 2016 Jan 14. pii: jbc.M115.691303. PMID:26769964<ref>PMID:26769964</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5c6c" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:17, 20 January 2016

2016-01-20T17:17:26Z

←Older revision		Revision as of 17:17, 20 January 2016
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==PKG II's Amino Terminal Cyclic Nucleotide Binding Domain (CNB-A) in a complex with cAMP==
-		+	<StructureSection load='5c6c' size='340' side='right' caption='[[5c6c]], [[Resolution\|resolution]] 2.05Å' scene=''>
-	~~The entry~~ 5c6c is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5c6c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6C FirstGlance]. <br>
-	~~Authors~~: ~~Campbell~~, J.C., ~~Reger, A~~.S., ~~Huang, G~~.Y., ~~Sankaran, B~~., ~~Kim, J~~.J., ~~Kim, C~~.W.	+	</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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </span></td></tr>
-	~~Description:~~	+	<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=5c6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6c OCA], [http://pdbe.org/5c6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6c RCSB], [http://www.ebi.ac.uk/pdbsum/5c6c PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
-	[[Category: ~~Reger~~, ~~A.S~~]]	+	__TOC__
-	[[Category: ~~Campbell~~, ~~J.C~~]]	+	</StructureSection>
-	[[Category: Kim, ~~J.J~~]]	+	[[Category: Transferase]]
-	[[Category: ~~Huang~~, ~~G.Y~~]]	+	[[Category: Campbell, J C]]
-	[[Category: ~~Kim~~, ~~C.W~~]]	+	[[Category: Huang, G Y]]
		+	[[Category: Kim, C W]]
		+	[[Category: Kim, J J]]
		+	[[Category: Reger, A S]]
	[[Category: Sankaran, B]]		[[Category: Sankaran, B]]
		+	[[Category: Binding site]]
		+	[[Category: Cyclic amp]]
		+	[[Category: Cyclic gmp]]
		+	[[Category: Cyclic gmp-dependent protein kinase type ii]]
		+	[[Category: Mutagenesis]]
		+	[[Category: Protein binding]]
		+	[[Category: Site-directed]]

OCA at 10:22, 16 December 2015

2015-12-16T10:22:12Z

←Older revision		Revision as of 10:22, 16 December 2015
Line 7:		Line 7:
	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Reger, A.S]]
		+	[[Category: Campbell, J.C]]
	[[Category: Kim, J.J]]		[[Category: Kim, J.J]]
	[[Category: Huang, G.Y]]		[[Category: Huang, G.Y]]
	[[Category: Kim, C.W]]		[[Category: Kim, C.W]]
	[[Category: Sankaran, B]]		[[Category: Sankaran, B]]
-	[[Category: Reger, A.S]]
-	[[Category: Campbell, J.C]]

OCA at 13:06, 29 July 2015

2015-07-29T13:06:42Z

←Older revision		Revision as of 13:06, 29 July 2015
Line 3:		Line 3:
	The entry 5c6c is ON HOLD		The entry 5c6c is ON HOLD

-	Authors: Campbell, J.C, ~~Kim~~, J.J, Huang, G.Y., ~~Reger~~, ~~A.s~~., ~~Sankaran~~, B, Kim, C.W.	+	Authors: Campbell, J.C., Reger, A.S., Huang, G.Y., Sankaran, B., Kim, J.J., Kim, C.W.

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Kim, J.J]]
		+	[[Category: Huang, G.Y]]
		+	[[Category: Kim, C.W]]
		+	[[Category: Sankaran, B]]
	[[Category: Reger, A.S]]		[[Category: Reger, A.S]]
-	~~[[Category: Sankaran, B, Kim, C.W]]~~	+	[[Category: Campbell, J.C]]
-	[[Category: Campbell, J.C~~, Kim, J.J, Huang, G.Y~~]]	+

OCA at 12:12, 15 July 2015

2015-07-15T12:12:44Z

←Older revision		Revision as of 12:12, 15 July 2015
Line 3:		Line 3:
	The entry 5c6c is ON HOLD		The entry 5c6c is ON HOLD

-	Authors: Campbell, J.C., ~~Reger~~, ~~A.S~~., Huang, G.Y., ~~Sankaran~~, B., ~~Kim~~, ~~J.J.~~, Kim, C.W.	+	Authors: Campbell, J.C, Kim, J.J, Huang, G.Y., Reger, A.s., Sankaran, B, Kim, C.W.

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Kim, J.J]]
-	[[Category: Huang, G.Y]]
-	[[Category: Kim, C.W]]
-	[[Category: Sankaran, B]]
	[[Category: Reger, A.S]]		[[Category: Reger, A.S]]
-	[[Category: Campbell, J.C]]	+	[[Category: Sankaran, B, Kim, C.W]]
		+	[[Category: Campbell, J.C, Kim, J.J, Huang, G.Y]]

OCA at 13:45, 8 July 2015

2015-07-08T13:45:49Z

←Older revision		Revision as of 13:45, 8 July 2015
Line 3:		Line 3:
	The entry 5c6c is ON HOLD		The entry 5c6c is ON HOLD

-	Authors: Campbell, J.C, Reger, A.s., Huang, G.Y., Sankaran, B, Kim, J.J, Kim, C.W.	+	Authors: Campbell, J.C., Reger, A.S., Huang, G.Y., Sankaran, B., Kim, J.J., Kim, C.W.

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Kim, J.J]]
	[[Category: Huang, G.Y]]		[[Category: Huang, G.Y]]
-	[[Category: ~~Campbell~~, J.C, Reger, A.S]]	+	[[Category: Kim, C.W]]
-	[[Category: ~~Sankaran, B, Kim~~, J.~~J, Kim,~~ C.W]]	+	[[Category: Sankaran, B]]
		+	[[Category: Reger, A.S]]
		+	[[Category: Campbell, J.C]]