5cvg - Revision history

OCA at 11:23, 10 January 2024

OCA — Wed, 10 Jan 2024 11:23:21 GMT

←Older revision		Revision as of 11:23, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5cvg]] is a 1 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=5CVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CVG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5cvg]] is a 1 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=5CVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CVG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 1.25Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [https://pdbe.org/5cvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [https://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg 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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [https://pdbe.org/5cvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [https://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:09, 21 June 2023

OCA — Wed, 21 Jun 2023 10:09:32 GMT

←Older revision		Revision as of 10:09, 21 June 2023
Line 3:		Line 3:
	<StructureSection load='5cvg' size='340' side='right'caption='[[5cvg]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='5cvg' size='340' side='right'caption='[[5cvg]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cvg]] is a 1 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=5CVG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CVG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cvg]] is a 1 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=5CVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CVG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [https://pdbe.org/5cvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [https://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg 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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [~~http~~://pdbe.org/5cvg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>	+	[https://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Brear P]]
-	[[Category: Brear, P]]	+	[[Category: De Fusco C]]
-	[[Category: Fusco, C De]]	+	[[Category: Georgiou KH]]
-	[[Category: Georgiou~~, K H~~]]	+	[[Category: Hyvonen M]]
-	[[Category: Hyvonen, M]]	+	[[Category: Spring D]]
-	[[Category: Spring, D]]	+
-	~~[[Category: Ck2a]]~~	+
-	~~[[Category: Ck2alpha]]~~	+
-	~~[[Category: Fragment based drug discovery]]~~	+
-	~~[[Category: High concentration screening]]~~	+
-	~~[[Category: Selective atp competitive inhibitor]]~~	+
-	~~[[Category: Surface entrophy reduction]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:26, 1 April 2020

OCA — Wed, 01 Apr 2020 10:26:08 GMT

←Older revision		Revision as of 10:26, 1 April 2020
Line 1:		Line 1:

	==Crystal Structure of CK2alpha with a novel closed conformation of the aD loop==		==Crystal Structure of CK2alpha with a novel closed conformation of the aD loop==
-	<StructureSection load='5cvg' size='340' side='right' caption='[[5cvg]], [[Resolution\|resolution]] 1.25Å' scene=''>	+	<StructureSection load='5cvg' size='340' side='right'caption='[[5cvg]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cvg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CVG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cvg]] is a 1 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=5CVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CVG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [http://pdbe.org/5cvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [http://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg 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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [http://pdbe.org/5cvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [http://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg ProSAT]</span></td></tr>
Line 21:		Line 22:

	==See Also==		==See Also==
-	*[[Casein kinase\|Casein kinase]]	+	*[[Casein kinase 3D structures\|Casein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Brear, P]]		[[Category: Brear, P]]

OCA at 06:21, 10 May 2017

OCA — Wed, 10 May 2017 06:21:47 GMT

←Older revision		Revision as of 06:21, 10 May 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>		[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The development of selective inhibitors of protein kinases is challenging because of the significant conservation of the ATP binding site. Here, we describe a new mechanism by which the protein kinase CK2alpha can be selectively inhibited using features outside the ATP site. We have identified a new binding site for small molecules on CK2alpha adjacent to the ATP site and behind the alphaD loop, termed the alphaD pocket. An elaborated fragment anchored in this site has been linked with a low affinity fragment binding in the ATP site, creating a novel and selective inhibitor (CAM4066) that binds CK2alpha with a Kd of 320 nM and shows significantly improved selectivity compared to other CK2alpha inhibitors. CAM4066 shows target engagement in several cell lines and similar potency to clinical trial candidate CX4945. Our data demonstrate that targeting a poorly conserved, cryptic pocket allows inhibition of CK2alpha via a novel mechanism, enabling the development of a new generation of selective CK2alpha inhibitors.
		+
		+	Specific inhibition of CK2alpha from an anchor outside the active site.,Brear P, De Fusco C, Hadje Georgiou K, Francis-Newton NJ, Stubbs CJ, Sore HF, Venkitaraman AR, Abell C, Spring DR, Hyvonen M Chem Sci. 2016 Nov 1;7(11):6839-6845. doi: 10.1039/c6sc02335e. Epub 2016 Jul 12. PMID:28451126<ref>PMID:28451126</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5cvg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Casein kinase\|Casein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:36, 27 July 2016

OCA — Wed, 27 Jul 2016 15:36:41 GMT

←Older revision		Revision as of 15:36, 27 July 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5cvg is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal Structure of CK2alpha with a novel closed conformation of the aD loop==
-		+	<StructureSection load='5cvg' size='340' side='right' caption='[[5cvg]], [[Resolution\|resolution]] 1.25Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5cvg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CVG FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5cvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvg OCA], [http://pdbe.org/5cvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cvg RCSB], [http://www.ebi.ac.uk/pdbsum/5cvg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvg ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Brear, P]]
		+	[[Category: Fusco, C De]]
		+	[[Category: Georgiou, K H]]
		+	[[Category: Hyvonen, M]]
		+	[[Category: Spring, D]]
		+	[[Category: Ck2a]]
		+	[[Category: Ck2alpha]]
		+	[[Category: Fragment based drug discovery]]
		+	[[Category: High concentration screening]]
		+	[[Category: Selective atp competitive inhibitor]]
		+	[[Category: Surface entrophy reduction]]
		+	[[Category: Transferase]]

OCA at 11:37, 15 May 2016

OCA — Sun, 15 May 2016 11:37:22 GMT

←Older revision		Revision as of 11:37, 15 May 2016
Line 3:		Line 3:
	The entry 5cvg is ON HOLD until Paper Publication		The entry 5cvg is ON HOLD until Paper Publication

-	Authors: ~~Brear, P., De Fusco, C., Georgiou, K.H., Spring, D., Hyvonen, M.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Hyvonen, M]]
-	[[Category: Brear, P]]
-	[[Category: Spring, D]]
-	[[Category: Georgiou, K.H]]
-	[[Category: De Fusco, C]]

OCA at 10:44, 16 December 2015

OCA — Wed, 16 Dec 2015 10:44:41 GMT

←Older revision		Revision as of 10:44, 16 December 2015
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Hyvonen, M]]		[[Category: Hyvonen, M]]
-	[[Category: Spring, D]]
-	[[Category: De Fusco, C]]
	[[Category: Brear, P]]		[[Category: Brear, P]]
		+	[[Category: Spring, D]]
	[[Category: Georgiou, K.H]]		[[Category: Georgiou, K.H]]
		+	[[Category: De Fusco, C]]

OCA: Protected "5cvg" [edit=sysop:move=sysop]

OCA — Wed, 05 Aug 2015 19:00:26 GMT

Protected "5cvg" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:00, 5 August 2015

OCA: New page: '''Unreleased structure''' The entry 5cvg is ON HOLD until Paper Publication Authors: Brear, P., De Fusco, C., Georgiou, K.H., Spring, D., Hyvonen, M. Description: [[Category: Unrelea...

OCA — Wed, 05 Aug 2015 19:00:24 GMT

New page: '''Unreleased structure''' The entry 5cvg is ON HOLD until Paper Publication Authors: Brear, P., De Fusco, C., Georgiou, K.H., Spring, D., Hyvonen, M. Description: [[Category: Unrelea...

New page

'''Unreleased structure'''

The entry 5cvg is ON HOLD until Paper Publication

Authors: Brear, P., De Fusco, C., Georgiou, K.H., Spring, D., Hyvonen, M.

Description:
[[Category: Unreleased Structures]]
[[Category: Hyvonen, M]]
[[Category: Spring, D]]
[[Category: De Fusco, C]]
[[Category: Brear, P]]
[[Category: Georgiou, K.H]]