3u87
Structure of a chimeric construct of human CK2alpha and human CK2alpha' in complex with a non-hydrolysable ATP-analogueStructure of a chimeric construct of human CK2alpha and human CK2alpha' in complex with a non-hydrolysable ATP-analogue
Template:ABSTRACT PUBMED 22868753
About this StructureAbout this Structure
3u87 is a 2 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3rp0. Full crystallographic information is available from OCA.
ReferenceReference
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- ↑ Bischoff N, Raaf J, Olsen B, Bretner M, Issinger OG, Niefind K. Enzymatic activity with an incomplete catalytic spine: insights from a comparative structural analysis of human CK2alpha and its paralogous isoform CK2alpha'. Mol Cell Biochem. 2011 Oct;356(1-2):57-65. Epub 2011 Jul 8. PMID:21739153 doi:10.1007/s11010-011-0948-5
- ↑ Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D. GTP plus water mimic ATP in the active site of protein kinase CK2. Nat Struct Biol. 1999 Dec;6(12):1100-3. PMID:10581548 doi:http://dx.doi.org/10.1038/70033
- ↑ Bischoff N, Olsen B, Raaf J, Bretner M, Issinger OG, Niefind K. Structure of the Human Protein Kinase CK2 Catalytic Subunit CK2alpha' and Interaction Thermodynamics with the Regulatory Subunit CK2beta. J Mol Biol. 2011 Mar 18;407(1):1-12. Epub 2011 Jan 15. PMID:21241709 doi:10.1016/j.jmb.2011.01.020
- ↑ Niefind K, Guerra B, Ermakowa I, Issinger OG. Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 2001 Oct 1;20(19):5320-31. PMID:11574463 doi:http://dx.doi.org/10.1093/emboj/20.19.5320
- ↑ Yde CW, Ermakova I, Issinger OG, Niefind K. Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate. J Mol Biol. 2005 Mar 25;347(2):399-414. Epub 2005 Jan 18. PMID:15740749 doi:http://dx.doi.org/10.1016/j.jmb.2005.01.003
- ↑ Niefind K, Yde CW, Ermakova I, Issinger OG. Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:17524418 doi:http://dx.doi.org/10.1016/j.jmb.2007.04.068
- ↑ Raaf J, Issinger OG, Niefind K. First inactive conformation of CK2 alpha, the catalytic subunit of protein kinase CK2. J Mol Biol. 2009 Mar 13;386(5):1212-21. Epub 2009 Jan 24. PMID:19361447 doi:10.1016/j.jmb.2009.01.033
- ↑ Raaf J, Brunstein E, Issinger OG, Niefind K. The CK2 alpha/CK2 beta interface of human protein kinase CK2 harbors a binding pocket for small molecules. Chem Biol. 2008 Feb;15(2):111-7. PMID:18291315 doi:http://dx.doi.org/10.1016/j.chembiol.2007.12.012
- ↑ Raaf J, Klopffleisch K, Issinger OG, Niefind K. The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin. J Mol Biol. 2008 Mar 14;377(1):1-8. Epub 2008 Jan 11. PMID:18242640 doi:http://dx.doi.org/10.1016/j.jmb.2008.01.008