Back Picture: Determination of Potential Scaffolds for Human Choline Kinase α1 by Chemical Deconvolution Studies (ChemBioChem 11/2013). Issue 11 (17th July 2013)

• Record Type: Journal Article
• Authors: Sahún‐Roncero, María; Rubio‐Ruíz, Belén; Conejo‐García, Ana; Velázquez‐Campoy, Adrián; Entrena, Antonio; Hurtado‐Guerrero, Ramon
• Is Part Of: Chembiochem. Volume 14:Issue 11(2013)
• Page Start: 1274
• Page End: 1388
• Publication Date: 2013-07-17
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201390041
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The back cover picture shows</bold> the the binding modes of a new CHOKa1 inhibitor. Using a chemical deconvolution approach based on the crystal structures of CHOKa1/1 and CHOKa1/2, A. Entrena, R. Hurtado‐Guerrero et al. have shown (<ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 1291 ff.</ext-link>) that adenine and 1‐benzyl‐4‐(dimethylamino)pyridinium are the most efficient fragments in the molecules and that CHOKa1 is very flexible, adopting local conformational changes in the choline binding site.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg2710jx0f" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>