3rps - Revision history

OCA at 09:44, 1 March 2024

OCA — Fri, 01 Mar 2024 09:44:24 GMT

←Older revision		Revision as of 09:44, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3rps' size='340' side='right'caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3rps' size='340' side='right'caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rps]] 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=3RPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([https://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'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [https://pdbe.org/3rps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [https://www.ebi.ac.uk/pdbsum/3rps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rps 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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [https://pdbe.org/3rps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [https://www.ebi.ac.uk/pdbsum/3rps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rps ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Eukaryotic protein kinases are fundamental factors for cellular regulation and therefore subject of strict control mechanisms. For full activity a kinase molecule must be penetrated by two stacks of hydrophobic residues, the regulatory and the catalytic spine that are normally well conserved among active protein kinases. We apply this novel spine concept here on CK2alpha, the catalytic subunit of protein kinase CK2. Homo sapiens disposes of two paralog isoforms of CK2alpha (hsCK2alpha and hsCK2alpha'). We describe two new structures of hsCK2alpha constructs one of which in complex with the ATP-analog adenylyl imidodiphosphate and the other with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol. The former is the first hsCK2alpha structure with a well defined cosubstrate/magnesium complex and the second with an open beta4/beta5-loop. Comparisons of these structures with existing CK2alpha/CK2alpha' and cAMP-dependent protein kinase (PKA) structures reveal: in hsCK2alpha' an open conformation of the interdomain hinge/helix alphaD region that is critical for ATP-binding is found corresponding to an incomplete catalytic spine. In contrast hsCK2alpha often adopts the canonical, PKA-like version of the catalytic spine which correlates with a closed conformation of the hinge region. HsCK2alpha can switch to the incomplete, non-canonical, hsCK2alpha'-like state of the catalytic spine, but this transition apparently depends on binding of either ATP or of the regulatory subunit CK2beta. Thus, ATP looks like an activator of hsCK2alpha rather than a pure cosubstrate.	+
-		+
-	Enzymatic activity with an incomplete catalytic spine: insights from a comparative structural analysis of human CK2alpha and its paralogous isoform CK2alpha'.,Bischoff N, Raaf J, Olsen B, Bretner M, Issinger OG, Niefind K Mol Cell Biochem. 2011 Oct;356(1-2):57-65. Epub 2011 Jul 8. PMID:21739153<ref>PMID:21739153</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3rps" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Bischoff N]]
-	[[Category: Bischoff, N]]	+	[[Category: Bretner M]]
-	[[Category: Bretner, M]]	+	[[Category: Issinger O-G]]
-	[[Category: Issinger, O G]]	+	[[Category: Niefind K]]
-	[[Category: Niefind, K]]	+	[[Category: Olsen B]]
-	[[Category: Olsen, B]]	+	[[Category: Raaf J]]
-	[[Category: Raaf, J]]	+
-	~~[[Category: Atp ck2beta]]~~	+
-	~~[[Category: Cytoplasm nucleus]]~~	+
-	~~[[Category: Eukaryotic protein kinase fold]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 10:21, 22 June 2022

OCA — Wed, 22 Jun 2022 10:21:04 GMT

←Older revision		Revision as of 10:21, 22 June 2022
Line 1:		Line 1:

	==Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol==		==Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol==
-	<StructureSection load='3rps' size='340' side='right' caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3rps' size='340' side='right'caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rps]] 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=3RPS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RPS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([https://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'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [~~http~~://pdbe.org/3rps PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rps PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rps 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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [https://pdbe.org/3rps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [https://www.ebi.ac.uk/pdbsum/3rps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rps 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 23:		Line 23:

	==See Also==		==See Also==
-	*[[Casein kinase\|Casein kinase]]	+	*[[Casein kinase 3D structures\|Casein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Bischoff, N]]		[[Category: Bischoff, N]]

OCA at 23:52, 4 August 2016

OCA — Thu, 04 Aug 2016 23:52:27 GMT

←Older revision		Revision as of 23:52, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol==		==Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol==
	<StructureSection load='3rps' size='340' side='right' caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3rps' size='340' side='right' caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RPS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rps]] 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=3RPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RPS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</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 ~~Homo sapiens~~])</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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [http://www.ebi.ac.uk/pdbsum/3rps 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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [http://pdbe.org/3rps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [http://www.ebi.ac.uk/pdbsum/3rps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rps ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3rps" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Bischoff, N]]		[[Category: Bischoff, N]]

OCA at 20:53, 24 December 2014

OCA — Wed, 24 Dec 2014 20:53:56 GMT

←Older revision		Revision as of 20:53, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}~~	+	==Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol==
-	===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===	+	<StructureSection load='3rps' size='340' side='right' caption='[[3rps]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21739153}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3rps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RPS FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4B0:3-(4,5,6,7-TETRABROMO-1H-BENZOTRIAZOL-1-YL)PROPAN-1-OL'>4B0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ofm\|3ofm]], [[1jwh\|1jwh]], [[3rp0\|3rp0]]</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 Homo sapiens])</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=3rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rps RCSB], [http://www.ebi.ac.uk/pdbsum/3rps PDBsum]</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>		[[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 ==
		+	Eukaryotic protein kinases are fundamental factors for cellular regulation and therefore subject of strict control mechanisms. For full activity a kinase molecule must be penetrated by two stacks of hydrophobic residues, the regulatory and the catalytic spine that are normally well conserved among active protein kinases. We apply this novel spine concept here on CK2alpha, the catalytic subunit of protein kinase CK2. Homo sapiens disposes of two paralog isoforms of CK2alpha (hsCK2alpha and hsCK2alpha'). We describe two new structures of hsCK2alpha constructs one of which in complex with the ATP-analog adenylyl imidodiphosphate and the other with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol. The former is the first hsCK2alpha structure with a well defined cosubstrate/magnesium complex and the second with an open beta4/beta5-loop. Comparisons of these structures with existing CK2alpha/CK2alpha' and cAMP-dependent protein kinase (PKA) structures reveal: in hsCK2alpha' an open conformation of the interdomain hinge/helix alphaD region that is critical for ATP-binding is found corresponding to an incomplete catalytic spine. In contrast hsCK2alpha often adopts the canonical, PKA-like version of the catalytic spine which correlates with a closed conformation of the hinge region. HsCK2alpha can switch to the incomplete, non-canonical, hsCK2alpha'-like state of the catalytic spine, but this transition apparently depends on binding of either ATP or of the regulatory subunit CK2beta. Thus, ATP looks like an activator of hsCK2alpha rather than a pure cosubstrate.

-	~~==About this Structure==~~	+	Enzymatic activity with an incomplete catalytic spine: insights from a comparative structural analysis of human CK2alpha and its paralogous isoform CK2alpha'.,Bischoff N, Raaf J, Olsen B, Bretner M, Issinger OG, Niefind K Mol Cell Biochem. 2011 Oct;356(1-2):57-65. Epub 2011 Jul 8. PMID:21739153<ref>PMID:21739153</ref>
-	~~[[3rps]] is a 2 chain structure~~ with ~~sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3RPS OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Casein kinase\|Casein kinase]]		*[[Casein kinase\|Casein kinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021739153</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Bischoff, N.]]	+	[[Category: Bischoff, N]]
-	[[Category: Bretner, M.]]	+	[[Category: Bretner, M]]
-	[[Category: Issinger, O G.]]	+	[[Category: Issinger, O G]]
-	[[Category: Niefind, K.]]	+	[[Category: Niefind, K]]
-	[[Category: Olsen, B.]]	+	[[Category: Olsen, B]]
-	[[Category: Raaf, J.]]	+	[[Category: Raaf, J]]
	[[Category: Atp ck2beta]]		[[Category: Atp ck2beta]]
	[[Category: Cytoplasm nucleus]]		[[Category: Cytoplasm nucleus]]

OCA at 08:28, 21 August 2013

OCA — Wed, 21 Aug 2013 08:28:59 GMT

←Older revision		Revision as of 08:28, 21 August 2013
Line 1:		Line 1:
-	[[Image:3rps.png\|left\|200px]]
-
	{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}		{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}
-
	===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===		===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===
		+	{{ABSTRACT_PUBMED_21739153}}

-	~~{{ABSTRACT_PUBMED_21241709}}~~	+	==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>

	==About this Structure==		==About this Structure==
Line 14:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~021241709~~</ref><~~ref~~ group="xtra"~~>PMID:011574463<~~/~~ref~~><references ~~group="xtra"~~/>	+	<ref group="xtra">PMID:021739153</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 09:02, 20 October 2012

OCA — Sat, 20 Oct 2012 09:02:28 GMT

←Older revision		Revision as of 09:02, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3rps]] is a 2 chain structure ~~of [[Casein kinase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA].	+	[[3rps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA].

	==See Also==		==See Also==

OCA at 21:35, 25 July 2012

OCA — Wed, 25 Jul 2012 21:35:17 GMT

←Older revision		Revision as of 21:35, 25 July 2012
Line 1:		Line 1:
-	[[Image:3rps.~~jpg~~\|left\|200px]]	+	[[Image:3rps.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3rps", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}		{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}

	===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===		===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21241709}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21241709 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21241709}}		{{ABSTRACT_PUBMED_21241709}}

	==About this Structure==		==About this Structure==
-	[[3rps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA].	+	[[3rps]] is a 2 chain structure of [[Casein kinase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA].
		+
		+	==See Also==
		+	*[[Casein kinase\|Casein kinase]]

	==Reference==		==Reference==
Line 31:		Line 23:
	[[Category: Olsen, B.]]		[[Category: Olsen, B.]]
	[[Category: Raaf, J.]]		[[Category: Raaf, J.]]
		+	[[Category: Atp ck2beta]]
		+	[[Category: Cytoplasm nucleus]]
		+	[[Category: Eukaryotic protein kinase fold]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 05:24, 8 June 2011

OCA — Wed, 08 Jun 2011 05:24:43 GMT

←Older revision		Revision as of 05:24, 8 June 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3rps.jpg\|left\|200px]]

-	The ~~entry 3rps~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3rps", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3rps\| PDB=3rps \| SCENE= }}

-	~~Authors: Bischoff~~, N., ~~Raaf~~, ~~J., Olsen, B., Bretner, M., Issinger, O.~~-~~G., Niefind, K.~~	+	===Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol===

-	~~Description: Structure of human CK2alpha in complex with the ATP~~-~~competitive inhibitor 3~~-(4,5,6,7-~~tetrabromo~~-1H-~~benzotriazol~~-~~1-yl)propan-1-ol~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21241709}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21241709 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21241709}}
		+
		+	==About this Structure==
		+	[[3rps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPS OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021241709</ref><ref group="xtra">PMID:011574463</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Bischoff, N.]]
		+	[[Category: Bretner, M.]]
		+	[[Category: Issinger, O G.]]
		+	[[Category: Niefind, K.]]
		+	[[Category: Olsen, B.]]
		+	[[Category: Raaf, J.]]

OCA: Protected "3rps" [edit=sysop:move=sysop]

OCA — Wed, 04 May 2011 06:35:49 GMT

Protected "3rps" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:35, 4 May 2011

OCA: New page: '''Unreleased structure''' The entry 3rps is ON HOLD Authors: Bischoff, N., Raaf, J., Olsen, B., Bretner, M., Issinger, O.-G., Niefind, K. Description: Structure of human CK2alpha in c...

OCA — Wed, 04 May 2011 06:35:48 GMT

New page: '''Unreleased structure''' The entry 3rps is ON HOLD Authors: Bischoff, N., Raaf, J., Olsen, B., Bretner, M., Issinger, O.-G., Niefind, K. Description: Structure of human CK2alpha in c...

New page

'''Unreleased structure'''

The entry 3rps is ON HOLD

Authors: Bischoff, N., Raaf, J., Olsen, B., Bretner, M., Issinger, O.-G., Niefind, K.

Description: Structure of human CK2alpha in complex with the ATP-competitive inhibitor 3-(4,5,6,7-tetrabromo-1H-benzotriazol-1-yl)propan-1-ol