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

María Sahún-Roncero, Belén Rubio-Ruiz, Giorgio Saladino, Ana Conejo-García, Antonio Espinosa, Adrián Velázquez-Campoy, Francesco Luigi Gervasio, Antonio Entrena, Ramon Hurtado-Guerrero

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)4582-6
Number of pages5
JournalAngewandte Chemie International Edition
Volume52
Issue number17
DOIs
Publication statusPublished - 22 Apr 2013

Keywords

  • Allosteric Regulation
  • Choline Kinase
  • Drug Design
  • Humans
  • Molecular Dynamics Simulation
  • Protein Conformation
  • Protein Kinase Inhibitors
  • X-Ray Diffraction

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