1m2q: Difference between revisions

Revision as of 23:05, 2 July 2008

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File:1m2q.png

Template:STRUCTURE 1m2q

Crystal structure of 1,8-di-hydroxy-4-nitro-xanten-9-one/CK2 kinase complexCrystal structure of 1,8-di-hydroxy-4-nitro-xanten-9-one/CK2 kinase complex

Template:ABSTRACT PUBMED 12419810

About this StructureAbout this Structure

1M2Q is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight., De Moliner E, Moro S, Sarno S, Zagotto G, Zanotti G, Pinna LA, Battistutta R, J Biol Chem. 2003 Jan 17;278(3):1831-6. Epub 2002 Nov 4. PMID:12419810

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of 1,8-di-hydroxy-4-nitro-xanten-9-one/CK2 kinase complex'''
+===Crystal structure of 1,8-di-hydroxy-4-nitro-xanten-9-one/CK2 kinase complex===
-==Overview==
+<!--
-Protein kinases play key roles in signal transduction and therefore are among the most attractive targets for drug design. The pharmacological aptitude of protein kinase inhibitors is highlighted by the observation that various diseases with special reference to cancer are because of the abnormal expression/activity of individual kinases. The resolution of the three-dimensional structure of the target kinase in complex with inhibitors is often the starting point for the rational design of this kind of drugs, some of which are already in advanced clinical trial or even in clinical practice. Here we present and discuss three new crystal structures of ATP site-directed inhibitors in complex with "casein kinase-2" (CK2), a constitutively active protein kinase implicated in a variety of cellular functions and misfunctions. With the help of theoretical calculations, we disclose some key features underlying the inhibitory efficiency of anthraquinone derivatives, outlining three different binding modes into the active site. In particular, we show that a nitro group in a hydroxyanthraquinone scaffold decreases the inhibitory constants K(i) because of electron-withdrawing and resonance effects that enhance the polarization of hydroxylic substituents in paraposition.
+The line below this paragraph, {{ABSTRACT_PUBMED_12419810}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12419810 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12419810}}
 ==About this Structure==
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 [[Category: Inhibitor-enzyme complex]]
 [[Category: Kinase]]
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