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Back Picture: Determination of Potential Scaffolds for Human Choline Kinase α1 by Chemical Deconvolution Studies (ChemBioChem 11/2013)
Author(s) -
SahúnRoncero María,
RubioRuíz Belén,
ConejoGarcía Ana,
VelázquezCampoy Adrián,
Entrena Antonio,
HurtadoGuerrero Ramon
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390041
Subject(s) - choline kinase , deconvolution , chemistry , pyridinium , molecule , stereochemistry , choline , chemical biology , cover (algebra) , combinatorial chemistry , biophysics , biochemistry , computer science , biology , organic chemistry , algorithm , engineering , phospholipid , membrane , phosphatidylcholine , mechanical engineering
The back cover picture shows 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 ( p. 1291 ff. ) 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.