2oxd: Difference between revisions

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[[Image:2oxd.png|left|200px]]

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~~'''~~Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors~~'''~~

===Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors===

~~==Overview==~~

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~~CK2 is a highly pleiotropic Ser/Thr protein kinase that is able~~ to ~~promote cell survival and enhance~~ the ~~tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K~~(~~i) values between 0~~.~~15 and 0~~.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, ~~in an area with a positive electrostatic potential that~~ is ~~able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining~~ the ~~ligand orientation and binding selectivity~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17768728}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17768728 is the PubMed ID number.

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==About this Structure==

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[[Category: Kinase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 11~~:51:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:47:35 2008''

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-[[Image:2oxd.jpg|left|200px]]
+{{Seed}}
+[[Image:2oxd.png|left|200px]]
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 {{STRUCTURE_2oxd|  PDB=2oxd  |  SCENE=  }}
-'''Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors'''
+===Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors===
-==Overview==
+<!--
-CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity.
+The line below this paragraph, {{ABSTRACT_PUBMED_17768728}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17768728 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17768728}}
 ==About this Structure==
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 [[Category: Kinase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:51:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:47:35 2008''