4rs6 - Revision history

OCA at 15:15, 8 November 2023

OCA — Wed, 08 Nov 2023 15:15:54 GMT

←Older revision		Revision as of 15:15, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
-	</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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [https://pdbe.org/4rs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 ProSAT]</span></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]] 2.6Å</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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [https://pdbe.org/4rs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 08:26, 8 March 2023

OCA — Wed, 08 Mar 2023 08:26:41 GMT

←Older revision		Revision as of 08:26, 8 March 2023
Line 3:		Line 3:
	<StructureSection load='4rs6' size='340' side='right'caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4rs6' size='340' side='right'caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLK2, SNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	</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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [https://pdbe.org/4rs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 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/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [~~http~~://pdbe.org/4rs6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN]] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>	+	[https://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:

	==See Also==		==See Also==
-	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Polo kinase]]~~	+	[[Category: Quan J]]
-	[[Category: Quan, J]]	+	[[Category: Shan H]]
-	[[Category: Shan, H]]	+	[[Category: Wang T]]
-	[[Category: Wang, T]]	+
-	~~[[Category: First pbd domain of polo like kinase ii]]~~	+
-	~~[[Category: Phosphorylation of target protein]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:42, 1 May 2019

OCA — Wed, 01 May 2019 09:42:34 GMT

←Older revision		Revision as of 09:42, 1 May 2019
Line 1:		Line 1:

	==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==		==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==
-	<StructureSection load='4rs6' size='340' side='right' caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='4rs6' size='340' side='right'caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLK2, SNK ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://pdbe.org/4rs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum]</span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://pdbe.org/4rs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Polo kinase]]		[[Category: Polo kinase]]
	[[Category: Quan, J]]		[[Category: Quan, J]]

OCA at 07:39, 20 June 2016

OCA — Mon, 20 Jun 2016 07:39:52 GMT

←Older revision		Revision as of 07:39, 20 June 2016
Line 1:		Line 1:
		+
	==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==		==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==
	<StructureSection load='4rs6' size='340' side='right' caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4rs6' size='340' side='right' caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4rs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://pdbe.org/4rs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN]] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>		[[http://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN]] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Polo-like kinase 2 (PLK2) is a crucial regulator in cell cycle progression, DNA damage response, and neuronal activity. PLK2 is characterized by the conserved N-terminal kinase domain and the unique C-terminal polo-box domain (PBD). The PBD mediates diverse functions of PLK2 by binding phosphorylated Ser-pSer/pThr motifs of its substrates. Here, we report the first crystal structure of the PBD of PLK2. The overall structure of the PLK2 PBD is similar to that of the PLK1 PBD, which is composed by two polo boxes each contain beta6alpha structures that form a 12-stranded beta sandwich domain. The edge of the interface between the two polo boxes forms the phosphorylated Ser-pSer/pThr motifs binding cleft. On the hand, the peripheral regions around the core binding cleft of the PLK2 PBD is distinct from that of the PLK1 PBD, which might confer the substrate specificity of the PBDs of the polo-like kinase family.
		+
		+	Crystal structure of the polo-box domain of polo-like kinase 2.,Shan HM, Wang T, Quan JM Biochem Biophys Res Commun. 2015 Jan 16;456(3):780-4. doi:, 10.1016/j.bbrc.2014.11.125. Epub 2014 Dec 13. PMID:25511705<ref>PMID:25511705</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4rs6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:11, 25 December 2014

OCA — Thu, 25 Dec 2014 10:11:47 GMT

←Older revision		Revision as of 10:11, 25 December 2014
Line 6:		Line 6:
	<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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN]] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:44, 3 December 2014

OCA — Wed, 03 Dec 2014 09:44:59 GMT

←Older revision		Revision as of 09:44, 3 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==
-		+	<StructureSection load='4rs6' size='340' side='right' caption='[[4rs6]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~The entry~~ 4rs6 is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4rs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
-	~~Authors~~: ~~Shan~~, H., Quan, J., Wang, T.	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure of the C~~ domain of ~~Polo~~ like ~~Kinase II in Homo Sapiens~~	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Polo kinase]]
		+	[[Category: Quan, J]]
		+	[[Category: Shan, H]]
		+	[[Category: Wang, T]]
		+	[[Category: First pbd domain of polo like kinase ii]]
		+	[[Category: Phosphorylation of target protein]]
		+	[[Category: Transferase]]

OCA at 06:45, 26 November 2014

OCA — Wed, 26 Nov 2014 06:45:53 GMT

←Older revision		Revision as of 06:45, 26 November 2014
Line 3:		Line 3:
	The entry 4rs6 is ON HOLD		The entry 4rs6 is ON HOLD

-	Authors: Shan, ~~Hongmei~~, Quan, ~~Junmin~~, Wang, ~~Tao~~	+	Authors: Shan, H., Quan, J., Wang, T.

	Description: Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens		Description: Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens

OCA: Protected "4rs6" [edit=sysop:move=sysop]

OCA — Wed, 19 Nov 2014 11:32:39 GMT

Protected "4rs6" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:32, 19 November 2014

OCA: New page: '''Unreleased structure''' The entry 4rs6 is ON HOLD Authors: Shan, Hongmei, Quan, Junmin, Wang, Tao Description: Crystal structure of the C domain of Polo like Kinase II in Homo Sapie...

OCA — Wed, 19 Nov 2014 11:32:38 GMT

New page: '''Unreleased structure''' The entry 4rs6 is ON HOLD Authors: Shan, Hongmei, Quan, Junmin, Wang, Tao Description: Crystal structure of the C domain of Polo like Kinase II in Homo Sapie...

New page

'''Unreleased structure'''

The entry 4rs6 is ON HOLD

Authors: Shan, Hongmei, Quan, Junmin, Wang, Tao

Description: Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens