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| - | [[Image:2rkp.gif|left|200px]]<br /> | + | #REDIRECT [[3h30]] This PDB entry is obsolete and replaced by 3h30 |
| - | <applet load="2rkp" size="450" color="white" frame="true" align="right" spinBox="true"
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| - | caption="2rkp, resolution 1.56Å" />
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| - | '''Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole'''<br />
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| - | ==Overview==
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| - | CK2alpha is the catalytic subunit of protein kinase CK2 and a member of, the CMGC family of eukaryotic protein kinases like the cyclin-dependent, kinases, the MAP kinases and glycogen-synthase kinase 3. We present here a, 1.6 A resolution crystal structure of a fully active C-terminal deletion, mutant of human CK2alpha liganded by two sulfate ions, and we compare this, structure systematically with representative structures of related CMGC, kinases. The two sulfate anions occupy binding pockets at the activation, segment and provide the structural basis of the acidic consensus sequence, S/T-D/E-X-D/E that governs substrate recognition by CK2. The anion binding, sites are conserved among those CMGC kinases. In most cases they are, neutralized by phosphorylation of a neighbouring threonine or tyrosine, side-chain, which triggers conformational changes for regulatory purposes., CK2alpha, however, lacks both phosphorylation sites at the activation, segment and structural plasticity. Here the anion binding sites are, functionally changed from regulation to substrate recognition. These, findings underline the exceptional role of CK2alpha as a constitutively, active enzyme within a family of strictly controlled protein kinases.
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| - | ==About this Structure==
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| - | 2RKP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL and RFZ as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2RKP OCA].
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| - | ==Reference==
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| - | 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., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-438. Epub 2007 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17524418 17524418]
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| - | [[Category: Homo sapiens]]
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| - | [[Category: Non-specific serine/threonine protein kinase]]
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| - | [[Category: Single protein]]
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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: CL]]
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| - | [[Category: RFZ]]
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| - | [[Category: allosteric binding site]]
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| - | [[Category: atp-binding]]
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| - | [[Category: drb]]
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| - | [[Category: eukaryotic protein kinase fold]]
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| - | [[Category: human ck2alpha]]
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| - | [[Category: nucleotide-binding]]
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| - | [[Category: protein kinase ck2]]
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| - | [[Category: protein kinase inhibitor complex]]
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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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:37:42 2007''
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