The mechanism of allosteric coupling in choline kinase α1 revealed by the action of a rationally designed inhibitor

Angew Chem Int Ed Engl. 2013 Apr 22;52(17):4582-6. doi: 10.1002/anie.201209660. Epub 2013 Feb 25.


Applying a CHOK hold: Combined experimental and computational studies of the binding mode of a rationally designed inhibitor of the dimeric choline kinase α1 (CHOKα1) explain the molecular mechanism of negative cooperativity (see scheme) and how the monomers are connected. The results give insight into how the symmetry of the dimer can be partially conserved despite a lack of conservation in the static crystal structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Choline Kinase / antagonists & inhibitors*
  • Choline Kinase / chemistry*
  • Choline Kinase / metabolism
  • Drug Design
  • Humans
  • Molecular Dynamics Simulation
  • Protein Conformation
  • Protein Kinase Inhibitors / chemistry*
  • Protein Kinase Inhibitors / pharmacology*
  • X-Ray Diffraction


  • Protein Kinase Inhibitors
  • Choline Kinase