3fwq: Difference between revisions

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[[Image:3fwq.png|left|200px]]
[[Image:3fwq.png|left|200px]]


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===Inactive conformation of human protein kinase CK2 catalytic subunit===
===Inactive conformation of human protein kinase CK2 catalytic subunit===


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Revision as of 02:09, 27 July 2012

File:3fwq.png

Template:STRUCTURE 3fwq

Inactive conformation of human protein kinase CK2 catalytic subunitInactive conformation of human protein kinase CK2 catalytic subunit

Template:ABSTRACT PUBMED 19361447

About this StructureAbout this Structure

3fwq is a 2 chain structure of Casein kinase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5][xtra 6][xtra 7][xtra 8][xtra 9][xtra 10]

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ 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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