1zoh

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Revision as of 08:27, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1zoh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zoh, resolution 1.81Å" /> '''Crystal structure of...)
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File:1zoh.gif


1zoh, resolution 1.81Å

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Crystal structure of protein kinase CK2 in complex with TBB-derivatives inhibitors

OverviewOverview

CK2 is a very pleiotropic protein kinase whose high constitutive activity, is suspected to cooperate to neoplasia. Here, the crystal structure of the, complexes between CK2 and three selective tetrabromo-benzimidazole, derivatives inhibiting CK2 with Ki values between 40 and 400 nM are, presented. The ligands bind to the CK2 active site in a different way with, respect to the parent compound TBB. They enter more deeply into the, cavity, establishing halogen bonds with the backbone of Glu114 and Val116, in the hinge region. A detailed analysis of the interactions highlights a, major role of the hydrophobic effect in establishing the rank of potency, within this class of inhibitors and shows that polar interactions are, responsible for the different orientation of the molecules in the active, site.

About this StructureAbout this Structure

1ZOH is a Single protein structure of sequence from Zea mays with NA, CL, K44 and EDO as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole., Battistutta R, Mazzorana M, Sarno S, Kazimierczuk Z, Zanotti G, Pinna LA, Chem Biol. 2005 Nov;12(11):1211-9. PMID:16298300

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