5otl - Revision history

OCA at 01:23, 28 December 2023

2023-12-28T01:23:56Z

←Older revision		Revision as of 01:23, 28 December 2023
Line 1:		Line 1:

	==The crystal structure of CK2alpha in complex with compound 29==		==The crystal structure of CK2alpha in complex with compound 29==
-	<StructureSection load='5otl' size='340' side='right' caption='[[5otl]], [[Resolution\|resolution]] 1.57Å' scene=''>	+	<StructureSection load='5otl' size='340' side='right'caption='[[5otl]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5otl]] 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=5OTL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5OTL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5otl]] 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=5OTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OTL 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>, <scene name='pdbligand=AQT:~{N}-[[3-chloranyl-4-(2-ethylphenyl)phenyl]methyl]-2-(5-methoxy-1~{H}-benzimidazol-2-yl)ethanamine'>AQT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.57Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AQT:~{N}-[[3-chloranyl-4-(2-ethylphenyl)phenyl]methyl]-2-(5-methoxy-1~{H}-benzimidazol-2-yl)ethanamine'>AQT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5otl OCA], [https://pdbe.org/5otl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5otl RCSB], [https://www.ebi.ac.uk/pdbsum/5otl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5otl 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=5otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5otl OCA], [~~http~~://pdbe.org/5otl PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5otl RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5otl PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5otl 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 22:		Line 21:

	==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: Homo sapiens]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: Brear, P]]	+	[[Category: Brear P]]
-	[[Category: Carro, L]]	+	[[Category: Carro L]]
-	[[Category: Fusco, C De]]	+	[[Category: De Fusco C]]
-	[[Category: Hyvonen, M]]	+	[[Category: Hyvonen M]]
-	[[Category: Iegre, J]]	+	[[Category: Iegre J]]
-	[[Category: Mitchell, S]]	+	[[Category: Mitchell S]]
-	[[Category: Rossmann, M]]	+	[[Category: Rossmann M]]
-	[[Category: Sore, H]]	+	[[Category: Sore H]]
-	[[Category: Spring, D]]	+	[[Category: Spring D]]
-	[[Category: Yoshida, M]]	+	[[Category: Yoshida M]]
-	~~[[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 05:50, 16 May 2018

2018-05-16T05:50:46Z

←Older revision		Revision as of 05:50, 16 May 2018
Line 3:		Line 3:
	<StructureSection load='5otl' size='340' side='right' caption='[[5otl]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='5otl' size='340' side='right' caption='[[5otl]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5otl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OTL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5otl]] 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=5OTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OTL 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>, <scene name='pdbligand=AQT:~{N}-[[3-chloranyl-4-(2-ethylphenyl)phenyl]methyl]-2-(5-methoxy-1~{H}-benzimidazol-2-yl)ethanamine'>AQT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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>, <scene name='pdbligand=AQT:~{N}-[[3-chloranyl-4-(2-ethylphenyl)phenyl]methyl]-2-(5-methoxy-1~{H}-benzimidazol-2-yl)ethanamine'>AQT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5otl OCA], [http://pdbe.org/5otl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5otl RCSB], [http://www.ebi.ac.uk/pdbsum/5otl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5otl 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=5otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5otl OCA], [http://pdbe.org/5otl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5otl RCSB], [http://www.ebi.ac.uk/pdbsum/5otl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5otl ProSAT]</span></td></tr>
Line 10:		Line 11:
	== 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 ==
		+	CK2 is a critical cell cycle regulator that also promotes various anti-apoptotic mechanisms. Development of ATP-non-competitive inhibitors of CK2 is a very attractive strategy considering that the ATP binding site is highly conserved among other kinases. We have previously utilised a pocket outside the active site to develop a novel CK2 inhibitor, CAM4066. Whilst CAM4066 bound to this new pocket it was also interacting with the ATP site: herein, we describe an example of a CK2alpha inhibitor that binds completely outside the active site. This second generation alphaD-site binding inhibitor, compound CAM4712 (IC50 = 7 muM, GI50 = 10.0 +/- 3.6 muM), has numerous advantages over the previously reported CAM4066, including a reduction in the number of rotatable bonds, the absence of amide groups susceptible to the action of proteases and improved cellular permeability. Unlike with CAM4066, there was no need to facilitate cellular uptake by making a prodrug. Moreover, CAM4712 displayed no drop off between its ability to inhibit the kinase in vitro (IC50) and the ability to inhibit cell proliferation (GI50).
		+
		+	Second-generation CK2alpha inhibitors targeting the alphaD pocket.,Iegre J, Brear P, De Fusco C, Yoshida M, Mitchell SL, Rossmann M, Carro L, Sore HF, Hyvonen M, Spring DR Chem Sci. 2018 Feb 20;9(11):3041-3049. doi: 10.1039/c7sc05122k. eCollection 2018 , Mar 21. PMID:29732088<ref>PMID:29732088</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5otl" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Casein kinase\|Casein kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Brear, P]]		[[Category: Brear, P]]

OCA at 06:21, 28 February 2018

2018-02-28T06:21:20Z

←Older revision		Revision as of 06:21, 28 February 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5otl ~~is ON HOLD until Paper Publication~~	+	==The crystal structure of CK2alpha in complex with compound 29==
-		+	<StructureSection load='5otl' size='340' side='right' caption='[[5otl]], [[Resolution\|resolution]] 1.57Å' scene=''>
-	~~Authors~~: ~~Brear, P~~., ~~De Fusco~~, C., ~~Iegre~~, J., ~~Yoshida~~, M., ~~Mitchell~~, S., ~~Rossmann~~, M., ~~Carro~~, L., ~~Sore~~, H., ~~Hyvonen~~, M., ~~Spring~~, D.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5otl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OTL FirstGlance]. <br>
-	~~Description~~: ~~The structure of CAM4703 bound to CK2alpha~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AQT:~{N}-[[3-chloranyl-4-(2-ethylphenyl)phenyl]methyl]-2-(5-methoxy-1~{H}-benzimidazol-2-yl)ethanamine'>AQT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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>
-	[[Category: ~~Yoshida~~, M]]	+	<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=5otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5otl OCA], [http://pdbe.org/5otl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5otl RCSB], [http://www.ebi.ac.uk/pdbsum/5otl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5otl 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: Carro, L]]
		+	[[Category: Fusco, C De]]
	[[Category: Hyvonen, M]]		[[Category: Hyvonen, M]]
-	[[Category: Rossmann, M]]
-	[[Category: Spring, D]]
	[[Category: Iegre, J]]		[[Category: Iegre, J]]
	[[Category: Mitchell, S]]		[[Category: Mitchell, S]]
-	[[Category: ~~De Fusco~~, ~~C]]~~	+	[[Category: Rossmann, M]]
-	~~[[Category: Brear, P~~]]	+
	[[Category: Sore, H]]		[[Category: Sore, H]]
-	[[Category: ~~Carro~~, L]]	+	[[Category: Spring, D]]
		+	[[Category: Yoshida, M]]
		+	[[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: Protected "5otl" [edit=sysop:move=sysop]

2017-09-27T12:50:22Z

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

←Older revision

Revision as of 12:50, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5otl is ON HOLD until Paper Publication Authors: Brear, P., De Fusco, C., Iegre, J., Yoshida, M., Mitchell, S., Rossmann, M., Carro, L., Sore, H., H...

2017-09-27T12:50:20Z

New page: '''Unreleased structure''' The entry 5otl is ON HOLD until Paper Publication Authors: Brear, P., De Fusco, C., Iegre, J., Yoshida, M., Mitchell, S., Rossmann, M., Carro, L., Sore, H., H...

New page

'''Unreleased structure'''

The entry 5otl is ON HOLD until Paper Publication

Authors: Brear, P., De Fusco, C., Iegre, J., Yoshida, M., Mitchell, S., Rossmann, M., Carro, L., Sore, H., Hyvonen, M., Spring, D.

Description: The structure of CAM4703 bound to CK2alpha
[[Category: Unreleased Structures]]
[[Category: Yoshida, M]]
[[Category: Hyvonen, M]]
[[Category: Rossmann, M]]
[[Category: Spring, D]]
[[Category: Iegre, J]]
[[Category: Mitchell, S]]
[[Category: De Fusco, C]]
[[Category: Brear, P]]
[[Category: Sore, H]]
[[Category: Carro, L]]