1f0q

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{{STRUCTURE_1f0q| PDB=1f0q | SCENE= }}
{{STRUCTURE_1f0q| PDB=1f0q | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''
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===CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN===
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==Overview==
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The structure of a complex between the catalytic subunit of Zea mays CK2 and the nucleotide binding site-directed inhibitor emodin (3-methyl-1,6,8-trihydroxyanthraquinone) was solved at 2.6-A resolution. Emodin enters the nucleotide binding site of the enzyme, filling a hydrophobic pocket between the N-terminal and the C-terminal lobes, in the proximity of the site occupied by the base rings of the natural co-substrates. The interactions between the inhibitor and CK2 alpha are mainly hydrophobic. Although the C-terminal domain of the enzyme is essentially identical to the ATP-bound form, the beta-sheet in the N-terminal domain is altered by the presence of emodin. The structural data presented here highlight the flexibility of the kinase domain structure and provide information for the design of selective ATP competitive inhibitors of protein kinase CK2.
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(as it appears on PubMed at http://www.pubmed.gov), where 10882732 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10882732}}
==About this Structure==
==About this Structure==
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[[Category: Zanotti, G.]]
[[Category: Zanotti, G.]]
[[Category: Protein kinase-inhibitor complex]]
[[Category: Protein kinase-inhibitor complex]]
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Revision as of 23:18, 30 June 2008

Image:1f0q.png

Template:STRUCTURE 1f0q

CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN

Template:ABSTRACT PUBMED 10882732

About this Structure

1F0Q is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2., Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA, J Biol Chem. 2000 Sep 22;275(38):29618-22. PMID:10882732

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