1f0q: Difference between revisions

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[[Image:1f0q.~~jpg~~|left|200px]]

[[Image:1f0q.png|left|200px]]

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

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

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10882732}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10882732 is the PubMed ID number.

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==About this Structure==

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[[Category: Zanotti, G.]]

[[Category: Protein kinase-inhibitor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:45:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:18:34 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1f0q.jpg|left|200px]]
+{{Seed}}
+[[Image:1f0q.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1f0q|  PDB=1f0q  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10882732}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10882732 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10882732}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Zanotti, G.]]
 [[Category: Protein kinase-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:45:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:18:34 2008''