3bqc

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{{STRUCTURE_3bqc| PDB=3bqc | SCENE= }}
{{STRUCTURE_3bqc| PDB=3bqc | SCENE= }}
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'''High pH-value crystal structure of emodin in complex with the catalytic subunit of protein kinase CK2'''
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===High pH-value crystal structure of emodin in complex with the catalytic subunit of protein kinase CK2===
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==Overview==
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The Ser/Thr kinase CK2 (former name: casein kinase 2) is a heterotetrameric enzyme composed of two catalytic chains (CK2alpha) attached to a dimer of noncatalytic subunits. Together with the cyclin-dependent kinases and the mitogen-activated protein kinases, CK2alpha belongs to the CMGC family of the eukaryotic protein kinases. CK2 is an important survival and stability factor in eukaryotic cells: its catalytic activity is elevated in a wide variety of tumors while its down-regulation can lead to apoptosis. Thus, CK2 is a valuable target for drug development and for chemical biology approaches of cell biological research, and small organic inhibitors addressing CK2 are of considerable interest. We describe here the complex structure between a C-terminal deletion mutant of human CK2alpha and the ATP-competitive inhibitor emodin (1,3,8-trihydroxy-6-methylanthraquinone, International Union of Pure and Applied Chemistry name: 1,3,8-trihydroxy-6-methylanthracene-9,10-dione) and compare it with a previously published complex structure of emodin and maize CK2alpha. With a resolution of 1.5 A, the human CK2alpha/emodin structure has a much better resolution than its maize counterpart (2.6 A). Even more important, in spite of a sequence identity of more than 77% between human and maize CK2alpha, the two structures deviate significantly in the orientation, in which emodin is trapped by the enzyme, and in the local conformations around the ligand binding site: maize CK2alpha shows its largest adaptations in the ATP-binding loop, whereas human CK2alpha shows its largest adaptations in the hinge region connecting the two main domains of the protein kinase core. These observations emphasize the importance of local plasticity for ligand binding and demonstrate that two orthologues of an enzyme can behave quite different in this respect.
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(as it appears on PubMed at http://www.pubmed.gov), where 18242640 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18242640}}
==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Wnt signaling pathway]]
[[Category: Wnt signaling pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:00:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:01:42 2008''

Revision as of 17:01, 27 July 2008

Image:3bqc.png

Template:STRUCTURE 3bqc

High pH-value crystal structure of emodin in complex with the catalytic subunit of protein kinase CK2

Template:ABSTRACT PUBMED 18242640

About this Structure

3BQC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin., Raaf J, Klopffleisch K, Issinger OG, Niefind K, J Mol Biol. 2008 Mar 14;377(1):1-8. Epub 2008 Jan 11. PMID:18242640

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