3fwq: Difference between revisions

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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 with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}^{[xtra 3]}^{[xtra 4]}^{[xtra 5]}^{[xtra 6]}^{[xtra 7]}^{[xtra 8]}^{[xtra 9]}

↑ 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
↑ 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, 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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OCA

[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, 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

[8] 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

[9] 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

[xtra 1]

[xtra 2]

[xtra 3]

[xtra 4]

[xtra 5]

[xtra 6]

[xtra 7]

[xtra 8]

[xtra 9]

@@ Line 8: / Line 8: @@
 ==About this Structure==
-[[3fwq]] 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=3FWQ OCA].
+[[3fwq]] 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=3FWQ OCA].
 ==See Also==
@@ Line 14: / Line 14: @@
 ==Reference==
-<ref group="xtra">PMID:019361447</ref><ref group="xtra">PMID:009564028</ref><ref group="xtra">PMID:010581548</ref><ref group="xtra">PMID:011574463</ref><ref group="xtra">PMID:012860116</ref><ref group="xtra">PMID:015740749</ref><ref group="xtra">PMID:016335523</ref><ref group="xtra">PMID:017524418</ref><ref group="xtra">PMID:018242640</ref><ref group="xtra">PMID:018291315</ref><references group="xtra"/>
+<ref group="xtra">PMID:019361447</ref><ref group="xtra">PMID:009564028</ref><ref group="xtra">PMID:010581548</ref><ref group="xtra">PMID:011574463</ref><ref group="xtra">PMID:012860116</ref><ref group="xtra">PMID:015740749</ref><ref group="xtra">PMID:017524418</ref><ref group="xtra">PMID:018242640</ref><ref group="xtra">PMID:018291315</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
 [[Category: Non-specific serine/threonine protein kinase]]

3fwq: Difference between revisions

Revision as of 19:53, 20 October 2012

Contents

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

About this StructureAbout this Structure

See AlsoSee Also

ReferenceReference

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3fwq: Difference between revisions

Revision as of 19:53, 20 October 2012

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

About this StructureAbout this Structure

See AlsoSee Also

ReferenceReference

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

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