1f0q
From Proteopedia
(New page: 200px<br /><applet load="1f0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f0q, resolution 2.63Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1f0q.jpg|left|200px]]<br /><applet load="1f0q" size=" | + | [[Image:1f0q.jpg|left|200px]]<br /><applet load="1f0q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f0q, resolution 2.63Å" /> | caption="1f0q, resolution 2.63Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''<br /> | '''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a complex between the catalytic subunit of Zea mays CK2 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1F0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with EMO as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1F0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=EMO:'>EMO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Zea mays]] | [[Category: Zea mays]] | ||
[[Category: Battistutta, R.]] | [[Category: Battistutta, R.]] | ||
| - | [[Category: Moliner, E | + | [[Category: Moliner, E De.]] |
[[Category: Papinutto, E.]] | [[Category: Papinutto, E.]] | ||
| - | [[Category: Pinna, L | + | [[Category: Pinna, L A.]] |
[[Category: Sarno, S.]] | [[Category: Sarno, S.]] | ||
[[Category: Zanotti, G.]] | [[Category: Zanotti, G.]] | ||
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[[Category: protein kinase-inhibitor complex]] | [[Category: protein kinase-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:35 2008'' |
Revision as of 10:33, 21 February 2008
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CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN
Overview
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.
About this Structure
1F0Q is a Single protein structure of sequence from Zea mays with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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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