Format

Send to

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

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

Author information

1
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.

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.

PMID:
23441033
DOI:
10.1002/anie.201209660
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center