3fwq

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'''Unreleased structure'''
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{{Seed}}
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[[Image:3fwq.jpg|left|200px]]
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The entry 3fwq is ON HOLD
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{{STRUCTURE_3fwq| PDB=3fwq | SCENE= }}
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Authors: Raaf, J., Issinger, O.-G., Niefind, K.
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===Inactive conformation of human protein kinase CK2 catalytic subunit===
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Description: Inactive conformation of human protein kinase CK2 catalytic subunit
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 11 12:35:47 2009''
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==About this Structure==
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3FWQ is a 2 chains structure of sequences 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=3FWQ OCA].
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==Reference==
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<ref group="xtra">PMID:9564028</ref><ref group="xtra">PMID:10581548</ref><ref group="xtra">PMID:11574463</ref><ref group="xtra">PMID:12860116</ref><ref group="xtra">PMID:15740749</ref><ref group="xtra">PMID:16335523</ref><ref group="xtra">PMID:17524418</ref><ref group="xtra">PMID:18242640</ref><ref group="xtra">PMID:18291315</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Issinger, O G.]]
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[[Category: Niefind, K.]]
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[[Category: Raaf, J.]]
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[[Category: Atp-binding]]
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[[Category: Casein kinase 2]]
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[[Category: Eukaryotic protein kinase]]
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[[Category: Inactive conformation]]
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[[Category: Kinase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protein kinase ck2]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Transferase]]
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[[Category: Wnt signaling pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:27:07 2009''

Revision as of 07:27, 18 February 2009

Image:3fwq.jpg

Template:STRUCTURE 3fwq

Inactive conformation of human protein kinase CK2 catalytic subunit

About this Structure

3FWQ is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Niefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. EMBO J. 1998 May 1;17(9):2451-62. PMID:9564028 doi:http://dx.doi.org/10.1093/emboj/17.9.2451
  • 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
  • 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
  • Ermakova I, Boldyreff B, Issinger OG, Niefind K. Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit. J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:12860116
  • 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, Issinger OG. Primary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme. Mol Cell Biochem. 2005 Jun;274(1-2):3-14. PMID:16335523
  • 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, 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
  • 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

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