2oxd: Difference between revisions

Revision as of 21:47, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oxd.png

Template:STRUCTURE 2oxd

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

Template:ABSTRACT PUBMED 17768728

About this StructureAbout this Structure

2OXD is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

ReferenceReference

The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules., Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA, Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:17768728

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OCA

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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.
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+{{ABSTRACT_PUBMED_17768728}}
 ==About this Structure==
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 [[Category: Kinase]]
 [[Category: Transferase]]
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