title: The mechanism of allosteric coupling in choline kinase α1 revealed by the action of a rationally designed inhibitor.
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.
authors: Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D; Fundacion ARAID, Edificio Pignatelli 36, Spain.
authors: María
authors: M
authors: Sahún-Roncero
authors: Belén
authors: B
authors: Rubio-Ruiz
authors: Giorgio
authors: G
authors: Saladino
authors: Ana
authors: A
authors: Conejo-García
authors: Antonio
authors: A
authors: Espinosa
authors: Adrián
authors: A
authors: Velázquez-Campoy
authors: Francesco Luigi
authors: FL
authors: Gervasio
authors: Antonio
authors: A
authors: Entrena
authors: Ramon
authors: R
authors: Hurtado-Guerrero
mesh_terms: D000494:Allosteric Regulation; D002797:Choline Kinase / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D015195:Drug Design; D006801:Humans; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D047428:Protein Kinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D014961:X-Ray Diffraction
chemical_list: D047428:Protein Kinase Inhibitors; D002797:Choline Kinase